It's made by hydrolyzing oils derived from—you guessed it—vegetables, and in all likeliness if you check your bathroom, it's in the fine print of your toothpaste and shampoo.
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After hydrolyzing one urea, this leaves glycolureate. After hydrolyzing the second urea, glycolaldehyde is left. Two glycolaldehydes condense to form erythrose 4-phosphate, which goes to the pentose phosphate shunt again.
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Syringic acid can be prepared by selectively hydrolyzing (demethylating) eudesmic acid with 20% sulfuric acid.
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N-acylethanolamine-hydrolyzing acid amidase is an enzyme that in humans is encoded by the NAAA gene. This gene encodes an N-acylethanolamine-hydrolyzing enzyme which is highly similar to acid ceramidase. Multiple transcript variants encoding different isoforms have been found for this gene.
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Glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1 is a protein that in humans is encoded by the QRSL1 gene.
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Kepone is made by dimerizing hexachlorocyclopentadiene and hydrolyzing to a ketone.Survey of Industrial Chemistry by Philip J. Chenier (2002), p. 484.
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Pyrethroid hydrolase (, pyrethroid-hydrolyzing carboxylesterase, pyrethroid- hydrolysing esterase, pyrethroid-hydrolyzing esterase, pyrethroid-selective esterase, pyrethroid-cleaving enzyme, permethrinase, PytH, EstP) is an enzyme with systematic name pyrethroid-ester hydrolase. This enzyme catalyses the following chemical reaction : trans-permethrin + H2O \rightleftharpoons (3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate The enzyme is involved in degradation of pyrethroid pesticides.
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One way hemolysin lyses erythrocytes is by forming pores in phospholipid bilayers. Other hemolysins lyse erythrocytes by hydrolyzing the phospholipids in the bilayer.
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KOR1 interacts with a two specific CesA proteins, possibly by proof-reading and relieving stress created by glucan chain synthesis, by hydrolyzing disordered amorphous cellulose.
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Potential avenues for the development of resistance to doripenem are: altered PBPs (penicillin-binding protein), reduced activity in the permeability of the outer membrane especially when accepting foreign toxic substances within the cell, and deactivation of the drug by hydrolyzing enzymes from the carbapenem. Beta-lactamases (such as penicillinases) formed by gram-positive and gram-negative bacteria can stabilize doripenem to hydrolysis. However, carbapenem-hydrolyzing beta-lactamases are an exception.
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The enzyme acts by hydrolyzing the terminal alpha-L-iduronic acid residues of these molecules, degrading them. The protein is reported as having a mass of approximately 83 kilodaltons.
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This results in narrower active site than the other alpha-amylase enzymes, which do not dimerize, and likely contributes to its ability of hydrolyzing both alpha-1,4- and alpha-1,6-glucosidic linkages.
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Both narrow spectrum beta- lactamases (e.g. penicillinases) and extended spectrum beta-lactamases (ESBL) are common for resistance plasmids in Enterobacteriaceae. Often multiple beta- lactamase genes are found on the same plasmid hydrolyzing a wide spectrum of beta-lactam antibiotics.
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Geobacillus thermoglucosidasius is a thermophilic gram-positive bacterium, and a member of the Firmicutes phylum. It was first isolated from soil in Japan in 1983. The species name thermoglucosidasius comes from the words therme denoting heat, and glucosidasius denoting starch-hydrolyzing glucosidase activity.
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One very common way to make potassium benzoate is by oxidizing toluene to benzoic acid followed by a neutralization with potassium hydroxide.Preparation of potassium benzoate, Another way to synthesize potassium benzoate in the lab setting is by hydrolyzing methyl benzoate with potassium hydroxide.
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Second, the open complex is extremely active and capable of quantitatively hydrolyzing all of the HPNP substrate in less than 40 min. By simply bubbling N2 into the solution, the reformation of the closed complex and the generation of an inactive catalyst can be achieved.
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S. humi reduces nitrogen. It is capable of hydrolyzing tween 20, arginine, and urea. It is oxidase positive, meaning that it produces cytochrome c oxidases. It is catalase negative, suggesting that it is incapable of forming catalase, and is therefore incapable of neutralizing hydrogen peroxide.
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Disproportionation is very similar to coupling, but the cleaved dextrin is not a cyclodextrin, but a linear oligosaccharide that is then joined to a second oligosaccharide. CGTase also has a weak hydrolyzing activity which consists in cleaving the longer polysaccharidic chains into shorter fragments.
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Herbert Zimmermann (born 10 January 1944) is a German neuroscientist who pioneered the studies on the biochemical, structural and functional heterogeneity of cholinergic synaptic vesicles from the electric organ of the electric ray Torpedo, and the functional and biochemical characterization of enzymes hydrolyzing extracellular nucleotides.
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The intestinal juice of Helix Pomatia contains large amounts of aryl, steroid and glucosinolate sulfatase activities. The sulfatases from the intestinal juice which have a broad specificity are commonly used as a hydrolyzing agent in analytical procedures like chromatography to prepare the sample for analysis.
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GTP-binding proteins, or G proteins, constitute a superfamily capable of binding GTP or GDP. G proteins are activated by binding GTP and are inactivated by hydrolyzing GTP to GDP. This general mechanism enables G proteins to perform a wide range of biologic activities.
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Dipeptidase 1 (DPEP1), or renal dipeptidase, is a membrane-bound glycoprotein responsible for hydrolyzing dipeptides. It is found in the microsomal fraction of the procine kidney cortex.Armstrong, David J., Sunil K. Mukhopadhyay, and Benedict J. Campbell. "Physicochemical characterization of renal dipeptidase." Biochemistry 13.8 (1974): 1745-750. Web.
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V-cath endopeptidase (, AcNPV protease, BmNPV protease, NPV protease, baculovirus cathepsin, nucleopolyhedrosis virus protease, viral cathepsin) is an enzyme. This enzyme catalyses the following chemical reaction : Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B This enzyme belongs to the peptidase family C1.
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NPP3 is probably a major contributor to nucleotide metabolism in the intestine and liver. Intestinal NPP3 would be involved in hydrolyzing food-derived nucleotides. The liver releases ATP and ADP into the bile to regulate bile secretion. It subsequently reclaims adenosine via a pathway that probably contains NPP3.
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Rats were administered a dosage of ethiofencarb, which was radio labeled, for 10 days and their urine was analyzed. It was found that 95% of the radioactivity was urinated out within 72 hours of administration. This chemical is rapidly oxidized in the bodies of mammals, hydrolyzing to phenolic metabolites.
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Glucose-6-Phosphate Translocase is a transmembrane protein providing a selective channel between the endoplasmic reticulum lumen and the cytosol. The enzyme is made up of three separate transporting subunits referred to as G6PT1 (subunit 1), G6PT2 (subunit 2) and G6PT3 (subunit 3). While the hydrolyzing component of the G6Pase complex is located on the side of the membrane on which it acts, namely facing the lumen, the translocases are all integral membrane proteins in order to perform their function as cross-membrane transporters. The translocases are spatially located on either side of the active site of the hydrolyzing component within the membrane, which allows the greatest speed and facility of the reaction.
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The prokaryotic phospholipase A2 domain is found in bacterial and fungal phospholipases. It enables the liberation of fatty acids and lysophospholipid by hydrolyzing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. The domain adopts an alpha-helical secondary structure, consisting of five alpha- helices and two helical segments.
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Aminoacylase 1 (ACY1: EC 3.5.14) is a zinc binding enzyme which hydrolyzes N-acetyl amino acids into the free amino acid and acetic acid. Of the N-acetyl amino hydrolyzing enzymes, aminoacylase 1 is the most common. The ACY1 gene is located on the short arm of chromosome 3 (3p21.2).
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Nitrogen oxides can also be used. Another way is by reacting 2,4-pentandedione with p-nitroso-N,N-dimethylaniline; forming an α-diazo-β- dicarbonyl derivative compound, and then reacting that with triphenylphosphine, and then hydrolyzing with sodium nitrite solution. Or the α-diazo-β-dicarbonyl derivative can be treated with tert-butylhypochlorite.
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When the residues at the entrance to the water channel were mutated to bulkier residues, such as Leucine, Phenylalanine or Tryptophan, the enzyme was no longer capable of hydrolyzing the LPA. This further supports the proposed mechanism in which water, supplied from the solvent through the channel, acts as a nucleophile in the active site.
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Bile Esculin Agar is used primarily to differentiate Enterococcus from Streptococcus. Members of the genus Enterococcus are capable of growing in the presence of 40% bile (oxgall) and hydrolyzing esculin to glucose and esculetin. Esculetin combines with ferric ions to produce a black complex. For some purposes, certain bacteria are able to hydrolyze aesculin.
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For potential applications to light emitting diodes, cubic silsesquioxanes. have been functionalized. One of the first precursors used in light emitting application was octadimethylsiloxysilsesquioxane, which can be prepared in yields of >90% by treating tetraethoxysilane or rice hull ash with tetramethylammonium hydroxide followed by dimethylchlorosilane. The general method of hydrolyzing organotrichlorosilanes is still effective here.
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In vivo, FtsZ forms filaments with a repeating arrangement of subunits, all arranged head-to-tail. These filaments form a ring around the longitudinal midpoint, or septum, of the cell. This ring is called the Z-ring. The GTP hydrolyzing activity of the protein is not essential to the formation of filaments or cell division.
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This translocase consists of the peripheral membrane ATPase SecA and the translocon membrane channel, which itself is composed of the proteins SecY, SecE, and SecG. Conformational changes within the SecA structure are the effect of its ATP- hydrolyzing behaviour and possibly lead to the stepwise export of the preprotein substrate through the SecYEG channel.
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When hydrolyzing a substrate, DPEP1 goes through a tetrahedral intermediate, after which the bridging solvent attacks the face of the carbonyl carbon of the scissile peptide bond.Thoden, James B., Ricardo Marti- Arbona, Frank M. Raushel, and Hazel M. Holden. "High-Resolution X-Ray Structure of Isoaspartyl Dipeptidase fromEscherichia coli†,‡." Biochemistry 42.17 (2003): 4874-882. Web.
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Other potential uses of metallacrowns in the body include hydrolyzing phosphate diesters, a key linkage component in RNA and DNA. Another part of the Pecoraro group research with metallacrowns focuses on their application as single-molecule magnet. Metallacryptate can be thought of as a metallacrown in three dimensions with a manganese oxide trapped in the middle.
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The long chain free fatty acids have the ability to prevent gastric lipase from hydrolyzing more triglycerides. In this case, gastric acid will be responsible for less than 30% of lipid hydrolysis. These enzymes are found in the cytoplasm and cell membranes of gastric cells. Gastric lipase is not the primary lipase needed for the majority of triglyceride hydrolysis.
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Light is emitted because the CoA synthesis pathway can be converted to the bioluminescence reaction by hydrolyzing the final product via an esterase back to D-luciferin. Luciferase activity is additionally inhibited by oxyluciferin and allosterically activated by ATP. When ATP binds to the enzyme’s two allosteric sites, luciferase’s affinity to bind ATP in its active site increases.
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N-acetylphosphatidylethanolamine-hydrolysing phospholipase D (, NAPE-PLD, anandamide-generating phospholipase D, N-acyl phosphatidylethanolamine phospholipase D, NAPE-hydrolyzing phospholipase D) is an enzyme with systematic name N-acetylphosphatidylethanolamine phosphatidohydrolase. This enzyme catalyses the following chemical reaction : N-acylphosphatidylethanolamine + H2O \rightleftharpoons N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate This enzyme is involved in the biosynthesis of anandamide.
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For movement between different compartments within the cell, vesicles rely on the motor proteins myosin, kinesin (primarily anterograde transport) and dynein (primarily retrograde transport). One end of the motor proteins attaches to the vesicle while the other end attaches to either microtubules or microfilaments. The motor proteins then move by hydrolyzing ATP, which propels the vesicle towards its destination.
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Retinyl ester hydrolysis requires the presence of bile salts that serve to solubilize the retinyl esters in mixed micelles and to activate the hydrolyzing enzymes Noy, N. (2006) "Vitamin A", "Biochemical, Physiological, & Molecular Aspects of Human Nutrition", M. H. Stipanuk 2nd Ed. Several enzymes that are present in the intestinal lumen may be involved in the hydrolysis of dietary retinyl esters. Cholesterol esterase is secreted into the intestinal lumen from the pancreas and has been shown, in vitro, to display retinyl ester hydrolase activity. In addition, a retinyl ester hydrolase that is intrinsic to the brush-border membrane of the small intestine has been characterized in the rat as well as in the human. The different hydrolyzing enzymes are activated by different types of bile salts and have distinct substrate specificities.
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The alpha subunit deactivates itself within minutes by hydrolyzing GTP to GDP (GTPase activity). The alpha subunit reassociates with beta-gamma dimer to form an inactive complex. A better understanding of the protein-ligand complex mechanisms may allow us for the treatment of some diseases such as type 2 diabetes. Glucagon receptor inhibitors are promising for the treatment of type 2 diabetes.
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Alkaline phosphatase primarily hydrolyzes phosphate monoester bonds, but it shows some promiscuity towards hydrolyzing phosphate diester bonds, making it a sort of opposite to NPP. The active sites of these two enzymes show marked similarities, namely in the presence of nearly superimposable Zn2+ bimetallo catalytic centers. In addition to the bimetallo core, AP also has an Mg2+ ion in its active site.
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ABHD6 is a serine hydrolyzing enzyme that possesses typical α/β-hydrolase family domains. ABHD6 was first studied because of its over-expression in certain forms of tumours. ABHD6 has been linked to regulation of the endocannabinoid system as it controls the accumulation of 2-arachidonoylglycerol (2-AG) at the cannabinoid receptors. ABHD6 accounts for about 4% of 2-AG brain hydrolysis.
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The details of NLK and ERK7 (MAPK15) activation remain unknown. Inactivation of MAPKs is performed by a number of phosphatases. A very conserved family of dedicated phosphatases is the so-called MAP kinase phosphatases (MKPs), a subgroup of dual-specificity phosphatases (DUSPs). As their name implies, these enzymes are capable of hydrolyzing the phosphate from both phosphotyrosine and the phosphothreonine residues.
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Enzymes serve a wide variety of functions inside living organisms. They are indispensable for signal transduction and cell regulation, often via kinases and phosphatases. They also generate movement, with myosin hydrolyzing ATP to generate muscle contraction, and also transport cargo around the cell as part of the cytoskeleton. Other ATPases in the cell membrane are ion pumps involved in active transport.
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Low molecular weight phosphotyrosine protein phosphatase is an enzyme that in humans is encoded by the ACP1 gene. The product of this gene belongs to the phosphotyrosine protein phosphatase family of proteins. It functions as an acid phosphatase and a protein tyrosine phosphatase by hydrolyzing protein tyrosine phosphate to protein tyrosine and orthophosphate. This enzyme also hydrolyzes orthophosphoric monoesters to alcohol and orthophosphate.
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Hydrogen bond acceptors, mostly nitrogen but also oxygen, reside in the ring system of the inhibitors. These atoms might interact with hydrogen bond donators, which are part of amino acids in the active site of the enzyme and thereby contribute to the inhibition of the enzyme from hydrolyzing cAMP and cGMP similar to how the natural substrates bind to the active site.
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The manganese-containing catalyst is used for the asymmetric epoxidation of alkenes. In the hydrolytic kinetic resolution technique, a racemic mixture of epoxides may be separated by selectively hydrolyzing one enantiomer, catalyzed by the analogous cobalt(III) complex. In subsequent work, chromium(III) and cobalt(III) salen complexes were found to be good catalysts for preparing polycarbonates from carbon dioxide and epoxides.
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They provided a cell biological explanation for a previously unresolved problem in the earlier history of neurotransmission, namely that newly synthesized acetylcholine is preferentially released form stimulated nerve endings. He further showed that ATP released from the electric nerves is hydrolyzed extracellularly to adenosine that is recycled via a high affinity transport mechanism into the nerve terminals where it is rephosphorylated and taken up in the form of ATP into synaptic vesicles. Starting from the observation that ATP is hydrolyzed extracellularly he analyzed the biochemical pathways leading to the extracellular breakdown of released nucleotides to their respective nucleosides. This resulted in the isolation and molecular cloning of the AMP- hydrolyzing enzyme ecto-5'-nucleotidase as well as of a number of the nucleoside triphosphate and diphosphate-hydrolyzing enzymes of the family of the ectonucleoside triphosphate diphosphohydrolases.
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Crystals of a DNase protein. A deoxyribonuclease (DNase, for short) is an enzyme that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA. Deoxyribonucleases are one type of nuclease, a generic term for enzymes capable of hydrolyzing phosphodiester bonds that link nucleotides. A wide variety of deoxyribonucleases are known, which differ in their substrate specificities, chemical mechanisms, and biological functions.
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The cycling of elements from dead organic matter by heterotrophic soil microorganisms is essential for nutrient turnover and energy transfer in terrestrial ecosystems. Exoenzymes also aid digestion in the guts of ruminants, termites, humans and herbivores. By hydrolyzing plant cell wall polymers, microbes release energy that has the potential to be used by humans as biofuel. Other human uses include waste water treatment, composting and bioethanol production.
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Fosfluconazole () is a water-soluble phosphate prodrug of fluconazole — a triazole antifungal drug used in the treatment and prevention of superficial and systemic fungal infections. The phosphate ester bond is hydrolyzed by the action of a phosphatase — an enzyme that removes a phosphate group from its substrate by hydrolyzing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (dephosphorylation).
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1.31) capable of hydrolyzing steroid β-glucuronides. Genetic variants in KLOTHO have been associated with human aging, and klotho protein has been shown to be a circulating factor detectable in serum that declines with age. The binding of certain fibroblast growth factors (FGF's, viz., FGF19 and FGF21) to their fibroblast growth factor receptors, is promoted via their interactions as co-receptors with β-klotho.
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Almost all of the variables required for protein synthesis affect mTORC1 activation by interacting with the TSC1/TSC2 protein complex. TSC2 is a GTPase activating protein (GAP). Its GAP activity interacts with a G protein called Rheb by hydrolyzing the GTP of the active Rheb-GTP complex, converting it to the inactive Rheb-GDP complex. The active Rheb-GTP activates mTORC1 through unelucidated pathways.
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Cellulase is used in the fermentation of biomass into biofuels, although this process is relatively experimental at present. Medically, Cellulase is used as a treatment for phytobezoars, a form of cellulose bezoar found in the human stomach, and it has exhibited efficacy in degrading polymicrobial bacterial biofilms by hydrolyzing the β(1-4) glycosidic linkages within the structural, matrix exopolysaccharides of the extracellular polymeric substance (EPS).
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Substitutes that increase the electron density promote the formation of the aldimin-tin chloride adduct. By electron withdrawing substituents, the formation of amide chloride is facilitated. In the past, the reaction was carried out by precipitating the aldimine-tin chloride, washing it with ether and then hydrolyzing it. However, it has been found that this step is unnecessary and the aldimine tin chloride can be hydrolysed directly in the solution.
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INPP5E is a phosphatidylinositol (3,4,5)-trisphosphate (PtdInsP3) and phosphatidylinositol 4,5-bisphosphate 5-phosphatase. Its intracellular localization is the primary cilium, a small organelle involved in signal transduction. INPP5E plays a role in hydrolyzing PtdInsP3 produced in response to various growth factors such as PDGF. Inactivation of the mouse INPP5E gene decreases primary cilia stability, leading to a multiorgan disorder, including absence of eyes, polydactyly, exencephaly and renal cysts.
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Collimonas is one of the species that are capable of living in the oligotrophic soil. One common feature of the environments where Collimonas lives is the presence of fungi, because Collimonas have the ability of not only hydrolyzing the chitin produced by fungi for nutrients, but also producing materials (e.g., P. fluorescens 2-79) to protect themselves from fungal infection. The mutual relationship is common in the oligotrophic environments.
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The purpose of completing the hydrolysis of dichlorosilane is to collect the concentrated hydrolysis products, distill the solution, and retrieve a solution of [H2SiO]n oligomers in dichloromethane. These methods were used to obtain cyclic polysiloxanes. Another purpose for hydrolyzing dichlorosilane is to obtain linear polysiloxanes, and can be done by many different complex methods. The hydrolysis of dichlorosilane in diethyl ether, dichloromethane, or pentane gives cyclic and linear polysiloxanes.
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The parotid gland also secretes salivary alpha-amylase (sAA), which is the first step in the decomposition of starches during mastication. It is the main exocrine gland to secrete this. It breaks down amylose (straight chain starch) and amylopectin (branched starch) by hydrolyzing alpha 1,4 bonds. Additionally, the alpha amylase has been suggested to prevent bacterial attachment to oral surfaces and to enable bacterial clearance from the mouth.
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The protein encoded by this gene belongs to the TDG/mug DNA glycosylase family. Thymine-DNA glycosylase (TDG) removes thymine moieties from G/T mismatches by hydrolyzing the carbon- nitrogen bond between the sugar-phosphate backbone of DNA and the mispaired thymine. With lower activity, this enzyme also removes thymine from C/T and T/T mispairings. TDG can also remove uracil and 5-bromouracil from mispairings with guanine.
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ParM is a prokaryotic actin homologue which provides the force to drive copies of the R1 plasmid to opposite ends of rod shaped bacteria before cytokinesis. ParM is a monomer that is encoded in the DNA of the R1 plasmid and manufactured by the host cell's ribosomes. In the cytoplasm it spontaneously polymerizes forming short strands that either bind to ParR or hydrolyze. ParR stabilizes ParM and prevents it from hydrolyzing.
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Many gene products that control mitochondrial fusion have been identified, and can be reduced to three core groups which also control mitochondrial fission. These groups of proteins include mitofusins, OPA1/Mgm1, and Drp1/Dnm1. All of these molecules are GTP hydrolyzing proteins (GTPases) that belong to the dynamin family. Mitochondrial dynamics in different cells are understood by the way in which these proteins regulate and bind to each other.
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X-linked inhibitor of apoptosis (XIAP) is hypothesized to promote cancer cell survival and growth. Macrophage inhibitory cytokine-1 (MIC-1) stimulates the focal adhesion kinase (FAK) signaling pathway which leads to cancer cell growth and survival. The androgen receptor helps cancer cells to survive. Prostate-specific membrane antigen (PSMA) stimulates cancer development by increasing folate levels, helping the cancer cells to survive and grow; it increases available folates for use by hydrolyzing glutamated folates.
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Betanin, or Beetroot Red, is a red glycosidic food dye obtained from beets; its aglycone, obtained by hydrolyzing away the glucose molecule, is betanidin. As a food additive, its E number is E162. The color of betanin depends on pH; between four and five it is bright bluish-red, becoming blue-violet as the pH increases. Once the pH reaches alkaline levels betanin degrades by hydrolysis, resulting in a yellow-brown color.
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GoLoco motif is a protein structural motif. In heterotrimeric G-protein signalling, cell surface receptors (GPCRs) are coupled to membrane-associated heterotrimers comprising a GTP-hydrolyzing subunit G-alpha and a G-beta/G-gamma dimer. The inactive form contains the alpha subunit bound to GDP and complexes with the beta and gamma subunit. When the ligand is associated to the receptor, GDP is displaced from G-alpha and GTP is bound.
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The biochemical mechanism that determines product length is not fully characterized. Although the three catalytic β subunits have a common mechanism, they have slightly different substrate specificities, which are considered chymotrypsin-like, trypsin-like, and peptidyl-glutamyl peptide- hydrolyzing (PHGH)-like. These variations in specificity are the result of interatomic contacts with local residues near the active sites of each subunit. Each catalytic β subunit also possesses a conserved lysine residue required for proteolysis.
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The pancreatic lipase acts at the ester bond, hydrolyzing the bond and "releasing" the fatty acid. In triglyceride form, lipids cannot be absorbed by the duodenum. Fatty acids, monoglycerides (one glycerol, one fatty acid), and some diglycerides are absorbed by the duodenum, once the triglycerides have been broken down. In the intestine, following the secretion of lipases and bile, triglycerides are split into monoacylglycerol and free fatty acids in a process called lipolysis.
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As an AAA+ ATPase, TRIP13 (and its PCH2 analog) forms homohexamers and interacts with ATP as an energy source. With respect to Hop1, PCH2 binds to and structurally changes Hop1, displacing the Hop1 from DNA. TRIP13/PCH2 interacts with ATP as a hydrolase, hydrolyzing phosphates to derive energy for conformational changes that can induce mechanical force on its substrate, Hop1 in the previous case. TRIP14/PCH2 is believed to have a single AAA+ ATPase domain.
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Pyroglutamyl-peptidase II (, thyroliberinase, pyroglutamyl aminopeptidase II, thyrotropin-releasing factor pyroglutamate aminopeptidase, pyroglutamate aminopeptidase II, pyroglutamyl peptidase II, thyroliberin-hydrolyzing pyroglutamate aminopeptidase, thyrotropin-releasing hormone-degrading pyroglutamate aminopeptidase, thyrotropin-releasing hormone-degrading peptidase, TRH aminopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction : Release of the N-terminal pyroglutamyl group from pGlu--His-Xaa tripeptides and pGlu--His-Xaa-Gly tetrapeptides This enzyme is highly specific for thyrotropin releasing hormone.
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Lysozymes act as bacteriolytic enzymes by hydrolyzing the beta(1->4) bonds between N-acetylglucosamine and N-acetylmuramic acid in the peptidoglycan of prokaryotic cell walls. It has also been recruited for a digestive role in certain ruminants and colobine monkeys. There are at least five different classes of lysozymes: C (chicken type), G (goose type), phage-type (T4), fungi (Chalaropsis), and bacterial (Bacillus subtilis). There are few similarities in the sequences of the different types of lysozymes.
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Rolipram, the prototypical PDE4 inhibitor A phosphodiesterase type 4 inhibitor, commonly referred to as a PDE4 inhibitor, is a drug used to block the degradative action of phosphodiesterase 4 (PDE4) on cyclic adenosine monophosphate (cAMP). It is a member of the larger family of PDE inhibitors. The PDE4 family of enzymes are the most prevalent PDE in immune cells. They are predominantly responsible for hydrolyzing cAMP within both immune cells and cells in the central nervous system.
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Hormone-sensitive lipase (, HSL), also previously known as cholesteryl ester hydrolase (CEH), sometimes referred to as triacylglycerol lipase, is an enzyme that, in humans, is encoded by the LIPE gene. HSL is an intracellular neutral lipase that is capable of hydrolyzing a variety of esters. The enzyme has a long and a short form. The long form is expressed in steroidogenic tissues such as testis, where it converts cholesteryl esters to free cholesterol for steroid hormone production.
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In enzymology, a coniferin beta-glucosidase () is an enzyme that catalyzes the chemical reaction :coniferin + H2O \rightleftharpoons D-glucose + coniferol Thus, the two substrates of this enzyme are coniferin and H2O, whereas its two products are D-glucose and coniferol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is coniferin beta-D- glucosidase. This enzyme is also called coniferin-hydrolyzing beta- glucosidase.
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Type I site-specific deoxyribonuclease (, type I restriction enzyme, deoxyribonuclease (ATP- and S-adenosyl-L-methionine-dependent), restriction- modification system, deoxyribonuclease (adenosine triphosphate-hydrolyzing), adenosine triphosphate-dependent deoxyribonuclease, ATP-dependent DNase, type 1 site-specific deoxyribonuclease) is an enzyme. This enzyme catalyses the following chemical reaction : Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolysed They have an absolute requirement for ATP (or dATP) and S-adenosyl- L-methionine.
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The product of this gene (the CFTR protein) is a chloride ion channel important in creating sweat, digestive juices, and mucus. This protein possesses two ATP-hydrolyzing domains, which allows the protein to use energy in the form of ATP. It also contains two domains comprising six alpha helices apiece, which allow the protein to cross the cell membrane. A regulatory binding site on the protein allows activation by phosphorylation, mainly by cAMP-dependent protein kinase.
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Outside of the stomach, gastric lipase can hydrolyze triacylglycerol in the duodenum with the help of other lipases and bile secretion. It is an essential enzyme for hydrolyzing milk fat globule membranes. For a newborn with an underdeveloped pancreas, LIPF plays a more important role in lipid digestion compared to an adult with a fully functioning pancreas. There is typically an increase in production of LIPF when the pancreas is unable to operate at its optimal potential.
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It can also be found in the cerebrospinal fluid when the meninges become inflamed (such as, for example, meningitis). Some ampicillin is metabolized by hydrolyzing the beta-lactam ring to penicilloic acid, though most of it is excreted unchanged. In the kidneys, it is filtered out mostly by tubular secretion; some also undergoes glomerular filtration, and the rest is excreted in the feces and bile. Hetacillin and pivampicillin are ampicillin esters that have been developed to increase bioavailability.
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MenH (SHCHC synthase) was previously thought to be a thioesterase involved in hydrolyzing DHNA-CoA in a later step of menaquinone synthesis. In 2008, it was determined that MenH has poor catalytic activity toward palmitoyl-CoA, casting doubt on its role as a thioesterase. Direct analysis confirmed that MenH is unable to hydrolyze DHNA-CoA. In 2009, it was proposed that a dedicated hotdog fold thioesterase would be needed to catalyze the hydrolysis of DHNA-CoA.
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Anabolism is powered by catabolism, where large molecules are broken down into smaller parts and then used up in cellular respiration. Many anabolic processes are powered by the cleavage of adenosine triphosphate (ATP). Anabolism usually involves reduction and decreases entropy, making it unfavorable without energy input. The starting materials, called the precursor molecules, are joined together using the chemical energy made available from hydrolyzing ATP, reducing the cofactors NAD+, NADP+, and FAD, or performing other favorable side reactions.
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Fernandez, C. W., McCormack, M. L., Hill, J. M., Pritchard, S. G., & Koide, R. T. (2013). On the persistence of Cenococcum geophilum ectomycorrhizas and its implications for forest carbon and nutrient cycles. Soil Biology and Biochemistry, 65, 141-143. This resistance to decay is likely related to the heavy melanization of the cell wall found in C. geophilum hyphae which cannot be degraded with hydrolyzing enzymes and requires the implementation of oxidative enzymes, much like lignin in plant litters.
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Arsenite resistance (Ars) efflux pumps of bacteria may consist of two proteins, ArsB (TC# 2.A.45.1.1; the integral membrane constituent with twelve transmembrane spanners) and ArsA (TC# 3.A.4.1.1; the ATP-hydrolyzing, transport energizing subunit, as for the chromosomally-encoded E. coli system), or of one protein (just the ArsB integral membrane protein of the plasmid-encoded Staphylococcus system). ArsA proteins have two ATP binding domains and probably arose by a tandem gene duplication event.
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Lactase is an enzyme that some people are unable to produce in their small intestine. Without it they cannot break down the natural lactose in milk, leaving them with diarrhea, gas and bloating when drinking regular milk. Technology to produce lactose-free milk, ice cream and yogurt was developed by the USDA Agricultural Research Service in 1985. This technology is used to add lactase to milk, thereby hydrolyzing the lactose naturally found in milk, leaving it slightly sweet but digestible by everyone.
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Ubiquitin carboxyl-terminal hydrolase 48 is an enzyme that in humans is encoded by the USP48 gene. This gene encodes a protein containing domains that associate it with the peptidase family C19, also known as family 2 of ubiquitin carboxyl-terminal hydrolases. Family members function as deubiquitinating enzymes, recognizing and hydrolyzing the peptide bond at the C-terminal glycine of ubiquitin. Enzymes in peptidase family C19 are involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
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GTPases are enzymes capable of binding and hydrolyzing guanosine triphosphate (GTP). Small GTPases, such as Ran and Ras, can exist in either a GTP-bound form (active) or a GDP-bound form (inactive), and the conversion between these two forms grants them a switch-like behavior. As such, small GTPases are involved in multiple cellular events, including nuclear translocation and signaling. The transition between the active and inactive states is facilitated by guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs).
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Numerous cyclic nucleotide phosphodiesterases (PDE) can degrade cGMP by hydrolyzing cGMP into 5'-GMP. PDE 5, -6 and -9 are cGMP- specific while PDE1, -2, -3, -10 and -11 can hydrolyse both cAMP and cGMP. Phosphodiesterase inhibitors prevent the degradation of cGMP, thereby enhancing and/or prolonging its effects. For example, Sildenafil (Viagra) and similar drugs enhance the vasodilatory effects of cGMP within the corpus cavernosum by inhibiting PDE 5 (or PDE V). This is used as a treatment for erectile dysfunction.
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Cholera gaining entry into a cell via endocytosis. As the endpoint of endocytosis, the lysosome also acts as a safeguard in preventing pathogens from being able to reach the cytoplasm before being degraded. Pathogens often hijack endocytotic pathways such as pinocytosis in order to gain entry into the cell. The lysosome prevents easy entry into the cell by hydrolyzing the biomolecules of pathogens necessary for their replication strategies; reduced Lysosomal activity results in an increase in viral infectivity, including HIV.
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S. pasteurii have the unique capability of hydrolyzing urea and through a series of reactions, produce carbonate ions. This is done by secreting copious amounts of urease through the cell membrane. When the bacterium is placed in a calcite rich environment, the negatively charged carbonate ions react with the positive metal ions like calcium to precipitate calcium carbonate, or bio-cement. The calcium carbonate can then be used as a precipitate or can be crystallized as calcite to cement sand particles together.
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The enzyme functions by attacking, hydrolyzing, and breaking glycosidic bonds in peptidoglycans. The enzyme can also break glycosidic bonds in chitin, although not as effectively as true chitinases. Overview of the reaction catalysed by lysozymeLysozymes active site binds the peptidoglycan molecule in the prominent cleft between its two domains. It attacks peptidoglycans (found in the cell walls of bacteria, especially Gram-positive bacteria), its natural substrate, between N-acetylmuramic acid (NAM) and the fourth carbon atom of N-acetylglucosamine (NAG).
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Whereas lanthanum oxyfluoride can be easily obtained by burning lanthanum trifluoride in air at 800 °C for an hour, similar treatment of actinium trifluoride yields no AcOF and only results in melting of the initial product.Meyer, pp. 87–88 :AcF3 \+ 2 NH3 \+ H2O → AcOF + 2 NH4F Actinium trichloride is obtained by reacting actinium hydroxide or oxalate with carbon tetrachloride vapors at temperatures above 960 °C. Similar to oxyfluoride, actinium oxychloride can be prepared by hydrolyzing actinium trichloride with ammonium hydroxide at 1000 °C.
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Sphingomyelin has been found to have a role in cell apoptosis by hydrolyzing into ceramide. Studies in the late 1990s had found that ceramide was produced in a variety of conditions leading to apoptosis. It was then hypothesized that sphingomyelin hydrolysis and ceramide signaling were essential in the decision of whether a cell dies. In the early 2000s new studies emerged that defined a new role for sphingomyelin hydrolysis in apoptosis, determining not only when a cell dies but how.
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Like many other black yeasts, C. carrionii is sensitive to temperatures above 37 °C. It can be distinguished in culture by the presence of its urease enzyme hydrolyzing urea and its inability to liquefy gelatin. Altering temperatures or micronutrient levels such as calcium and phosphate affects whether C. carrionii is in the mycelial or muriform state. The fungus transforms to muriform cells under conditions of temperature between 25 °C to 37 °C, 0.1 mM Ca2+, and a pH of 2.5.
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Phospholipases A2 (PLA2s) are enzymes that cleave fatty acid in position two of phospholipids, hydrolyzing the bond between the second fatty acid “tail” and the glycerol molecule. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond, releasing arachidonic acid and lysophosphatidic acid. Upon downstream modification by cyclooxygenases or lipoxygenases, arachidonic acid is modified into active compounds called eicosanoids. Eicosanoids include prostaglandins and leukotrienes, which are categorized as anti-inflammatory and inflammatory mediators.
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The ATP hydrolyzing activity is indispensable for the p97/CDC48 functions. The two ATPase domains of p97 (D1 and D2) are not equivalent because the D2 domain displays higher ATPase activity than the D1 domain in wild-type protein. Nevertheless, their activities are dependent of each other. For example, nucleotide binding to the D1 domain is required for ATP binding to the D2 domain and nucleotide binding and hydrolysis in D2 is required for the D1 domain to hydrolyze ATP.
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In enzymology, an oligosaccharide 4-alpha-D-glucosyltransferase () is an enzyme that catalyzes the chemical reaction in which the non-reducing terminal alpha-D-glucose residue is transferred from a 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan. This enzyme is useful in hydrolyzing oligosaccharides. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase.
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Spontaneous branch migration can occur, however, as it generally proceeds equally in both directions it is unlikely to complete recombination efficiently. The RecA protein catalyzes unidirectional branch migration and by doing so makes it possible to complete recombination, producing a region of heteroduplex DNA that is thousands of base pairs long. Since it is a DNA-dependent ATPase, RecA contains an additional site for binding and hydrolyzing ATP. RecA associates more tightly with DNA when it has ATP bound than when it has ADP bound.
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Each monomer comprises four distinct α/β structural units, each of which contains one of the four strands in each monomer's β-sheet and is made up only of the residues in a given sequence domain (see image at right). The burial of the active site (including Ser-116, the critical residue on the enzyme that is phosphorylated and dephosphorylated) in the hydrophobic interior of the enzyme serves to exclude water from counterproductively hydrolyzing critical phosphoester bonds while still allowing the substrate to access the active site.
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Neurolysin, mitochondrial is a protein that in humans is encoded by the NLN gene. It is a 78-kDa enzyme, widely distributed in mammalian tissues and found in various subcellular locations that vary with cell type. Neurolysin exemplifies the ability of neuropeptidases to target various cleavage site sequences by hydrolyzing them in vitro, and metabolism of neurotensin is the most important role of neurolysin in vivo. Neurolysin has also been implicated in pain control, blood pressure regulation, sepsis, reproduction, cancer biology pathogenesis of stroke, and glucose metabolism.
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Paraoxonases have been found to perform a number of biological functions, though the primary role of this group of enzymes is still a topic of speculation. Some of the observed roles have revealed activities of anti-inflammatory, anti-oxidative, anti- atherogenic, anti-diabetic, anti-microbial and organophosphate-hydrolyzing properties.Aggarwal G, Prajapati R, Tripathy RK, Bajaj P, Iyengar ARS, Sangamwar AT, et al. (2016) Toward Understanding the Catalytic Mechanism of Human Paraoxonase 1: Site-Specific Mutagenesis at Position 192. PLoS ONE 11(2): e0147999. doi:10.1371/journal.pone.
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This modification generates the binding site for the phosphatase, a SH2 recognition domain. The abrogation of ITAM activation signaling is caused by inhibition of protein tyrosine kinases of Src family, and by hydrolyzing the membrane PIP3 interrupting the further downstream signaling by the activating receptors, such as activating FcγRs, TCR, BCR and cytokine receptors (e.g. c-Kit). The negative signaling by FcγRIIB is mainly important for regulation of activated B cells. The positive B cell signaling is initiated by binding of foreign antigen to surface immunoglobulin.
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During neurotransmission, ACh is released from the presynaptic neuron into the synaptic cleft and binds to ACh receptors on the post-synaptic membrane, relaying the signal from the nerve. AChE, also located on the post- synaptic membrane, terminates the signal transmission by hydrolyzing ACh. The liberated choline is taken up again by the pre-synaptic neuron and ACh is synthesized by combining with acetyl-CoA through the action of choline acetyltransferase. A cholinomimetic drug disrupts this process by acting as a cholinergic neurotransmitter that is impervious to acetylcholinesterase's lysing action.
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In enzymology, a lysophospholipase () is an enzyme that catalyzes the chemical reaction :2-lysophosphatidylcholine + H2O \rightleftharpoons glycerophosphocholine + a carboxylate Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This family consists of lysophospholipase / phospholipase B and cytosolic phospholipase A2 which also has a C2 domain . Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells.
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Silk amino acid (SAAs) also known as Sericin is a natural water-soluble glycoprotein extracted from raw silk. It is used as an additive in skin and hair care products due to its high levels of serine which has excellent moisture preservation characteristics. As a water-based additive it is used to provide a protective barrier and silky feel to lotions, soaps, personal lubricants, hair and skincare products. Silk amino acids are produced by hydrolyzing (or breaking apart) silk proteins into smaller peptide chains, typically 18 to 19 amino acids in length.
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Autolysins breaks down old peptidoglycan which allows for the formation of newer peptidoglycan for cell growth and elongation. This is called cell wall turnover. Autolysins do this by hydrolyzing the β-(1,4) glycosidic bond of the peptidoglycan cell wall and the linkage between N-acetylmuramoyl residues and L-amino acid residues of certain cell-wall glycopeptides . This enzyme catalyses the following chemical reaction: : Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-Arg- Phe-Ala This glycoprotein is present in Chlamydomonas reinhardtii gametes.
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Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing) (, PdxST) is an enzyme with systematic name D-ribose 5-phosphate,D-glyceraldehyde 3-phosphate pyridoxal 5'-phosphate-lyase. This enzyme catalyses the following chemical reaction : D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine \rightleftharpoons pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate (overall reaction) :(1a) L-glutamine + H2O \rightleftharpoons L-glutamate + NH3 :(1b) D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3 \rightleftharpoons pyridoxal 5'-phosphate + 4 H2O + phosphate The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate.
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People with OI are born with defective connective tissue, or without the ability to make it, usually because of a deficiency of Type-I collagen. This deficiency arises from an amino acid substitution of glycine to bulkier amino acids in the collagen triple helix structure. The larger amino acid side-chains create steric hindrance that creates a bulge in the collagen complex, which in turn influences both the molecular nanomechanics and the interaction between molecules, which are both compromised. As a result, the body may respond by hydrolyzing the improper collagen structure.
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Glycerol 3-phosphate is synthesized by reducing dihydroxyacetone phosphate (DHAP), a glycolysis intermediate, with glycerol-3-phosphate dehydrogenase. DHAP and thus glycerol 3-phosphate is also possible to be synthesized from amino acids and citric acid cycle intermediates via glyceroneogenesis pathway. :DHAP + NAD(P)H + H+ → G1P + NAD(P)+ It is also synthesized by phosphorylating glycerol generated upon hydrolyzing fats with glycerol kinase, and can feed into glycolysis or gluconeogenesis pathways. :Glycerol + ATP → G3P + ADP Glycerol 3-phosphate is a starting material for de novo synthesis of glycerolipids.
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The enzyme requires a two-molecule metal cluster of manganese in order to maintain proper function. These Mn2+ ions coordinate with water, orienting and stabilizing the molecule and allowing water to act as a nucleophile and attack L-arginine, hydrolyzing it into ornithine and urea. In most mammals, two isozymes of this enzyme exist; the first, Arginase I, functions in the urea cycle, and is located primarily in the cytoplasm of hepatocytes (liver cells). The second isozyme, Arginase II, has been implicated in the regulation of intracellular arginine/ornithine levels.
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B. thetaiotaomicron is capable of metabolizing a very diverse range of polysaccharides. Its complement of enzymes for hydrolysis of glycosidic bonds is among the largest known in prokaryotes, and it is thought to be capable of hydrolyzing most glycosidic bonds in biological polysaccharides. As a component of the human gut flora, it can use both dietary carbohydrates and those sourced from the host, depending on nutrient availability. Although it is considered an obligate anaerobe, B. thetaiotaomicron is aerotolerant and can survive, but not grow, when exposed to oxygen.
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This potentially leads to cell death and is the reason why ADEP is a promising technique for drug development. For folded proteins, unfolded proteins, and long peptides, ClpP must be activated by a protein in the family of ATPase associated with diverse cellular activities (AAA proteins), such as ClpA, ClpX, or ClpC. These chaperone proteins are responsible for hydrolyzing ATP to ADP, harnessing the energy, and then taking folded proteins and unfolding them. Next, Clp-ATPases slip the unfolded proteins into the degradation chamber within ClpP, allowing for processive degradation of the substrate.
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Pectin is the soluble polymeric material in the pulp of oranges, which contains 75% of carboxyl of arabinose and galactose. Pectic compounds are complex heteropolysaccharides in that their chemical composition includes a chain structure of axial-axial α-1.4-linked d-galacturonic acid unit along with blocks of L-rhamnose regions that have side chains of arabinose, galactose, and xylose. Pectin methyl-esterase is the enzyme responsible for hydrolyzing carboxymethyl esters and liberating free carboxyl groups and methyl alcohols. The free carboxyl groups interact with cations to form insoluble pectic acid divalent metal ion complexes.
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Amylase reaction consisting of hydrolyzing amylose, producing maltose Maltose (Dictionary Reference: maltose or Cambridge dictionary: maltose), also known as maltobiose or malt sugar, is a disaccharide formed from two units of glucose joined with an α(1→4) bond. In the isomer isomaltose, the two glucose molecules are joined with an α(1→6) bond. Maltose is the two-unit member of the amylose homologous series, the key structural motif of starch. When beta- amylase breaks down starch, it removes two glucose units at a time, producing maltose.
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The addition of PPDK to the conversion of phosphoenolpyruvate to pyruvate (typically catalyzed solely by pyruvate kinase) has a strong effect on ATP conservation. Both PFP and PPDK rely on inorganic phosphate (PPi) as the phosphate donor; therefore rather than hydrolyzing ATP, the ATP yield is increased by using a by-product of the cell's anabolic processes as an energy source. These reactions are able to allow for greater ATP conservation and regulation of glycolysis due to the PPDK's reversible nature and use of inorganic phosphate where pyruvate kinase only catalyzes the forward reaction.
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OBPgp279 (OBP genome protein 279) is an endolysin that hydrolyzes peptidoglycan, a major constituent in bacterial membrane. OBPgp279 is found in Pseudomonas fluorescens phage OBP, which belongs in the Myoviridae family of bacteriophages. Because of its role in hydrolyzing the peptidoglycan layer, OBPgp279 is a key enzyme in the lytic cycle of the OBP bacteriophage; it allows the bacteriophage to lyse its host internally to escape. Unlike other endolysins, OBPgp279 does not rely on holins to perforate the inner bacterial membrane in order to reach the peptidoglycan layer.
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Ideal lipase growth conditions in Aspergillus wentii (100% lipase activity) occur under media supplemented with glucose of pH 6.0 at a temperature of 30 °C. Aspergillus wentii grown in mannitol media produces the second largest lipase yield (with 84% lipase activity). Lipase activity for Aspergillus wentii grown on fructose media produces just under 50% lipase activity while media supplemented with galactose, sucrose, lactose or maltose all yielded moderate lipase activity (20-37%). Aspergillus wentii strain NRRL 2001 spores were found to naturally produce glucose from hydrolyzing soluble starch.
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Ideonella sakaiensis cells adhere to the PET surface and use a secreted PET hydrolase, or PETase, to degrade the PET into mono(2-hydroxyethyl)terephthalic acid (MHET), a heterodimer composed of terephthalic acid (TPA) and ethylene glycol. The I. sakaiensis PETase functions by hydrolyzing the ester bonds present in PET with high specificity. The resulting MHET is then degraded into its two monomeric constituents by a lipid-anchored MHET hydrolase enzyme, or MHETase, on the cell's outer membrane. Ethylene glycol is readily taken up and used by I. sakaiensis and many other bacteria.
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It allows bacteria to adhere to host surfaces, protects the bacterial cells from host defenses, results in increased resistance to antibiotics, and provides a protected environment with microchannels for the flow of water and other essential nutrients. By hydrolyzing PGA, Dispersin B disrupts the formation of the biofilm matrix and allows adherent cells to be released. Dispersin B has also been shown to cause the detachment of biofilm cells that have adhered to abiotic surfaces as well as cause the disaggregaton of highly auto-aggregated clumps of bacterial cells.
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Glycoside hydrolase family 29 includes alpha-L-fucosidases, They are lysosomal enzymes responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Fucosylated glycoconjugates are involved in numerous biological events, making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. Deficiency in alpha-l-fucosidase activity is associated with fucosidosis, a lysosomal storage disorder characterised by rapid neurodegeneration, resulting in severe mental and motor deterioration.
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Excision endonuclease, also known as excinuclease or UV-specific endonuclease, is a nuclease (enzyme) which excises a fragment of nucleotides during DNA repair. The excinuclease cuts out a fragment by hydrolyzing two phosphodiester bonds, one on either side of the lesion in the DNA. This process is part of "nucleotide excision repair", a mechanism that can fix specific types of damage to the DNA in the G1 phase of the eukaryotic cell cycle. Such damage may include thymine dimers created by UV rays as well as the bulky distortions in DNA caused by oxidized benzopyrenes from sources such as cigarette smoke.
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Such observations are due to, primarily, steric effects. Steric hinderance is provided for by specific side chain groups of amino acids, which aids in inhibiting intermolecular attacks on the ester carbonyl; these intermolecular attacks are responsible for hydrolyzing the ester bond. Branched and aliphatic amino acids (valine and isoleucine) prove to generate the most stable aminoacyl-tRNAs upon their synthesis, with notably longer half lives than those that possess low hydrolytic stability (for example, proline). The steric hinderance of valine and isoleucine amino acids is generated by the methyl group on the β-carbon of the side chain.
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3′ to 5′ Exonuclease associated with Pol I Exonucleases are enzymes that work by cleaving nucleotides one at a time from the end (exo) of a polynucleotide chain. A hydrolyzing reaction that breaks phosphodiester bonds at either the 3′ or the 5′ end occurs. Its close relative is the endonuclease, which cleaves phosphodiester bonds in the middle (endo) of a polynucleotide chain. Eukaryotes and prokaryotes have three types of exonucleases involved in the normal turnover of mRNA: 5′ to 3′ exonuclease (Xrn1), which is a dependent decapping protein; 3′ to 5′ exonuclease, an independent protein; and poly(A)-specific 3′ to 5′ exonuclease.
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Although most operons in DNA are Rho independent, Rho dependent termination is also essential to maintain correct transcription. ρ factor The Rho protein is an RNA translocase that recognizes a cytosine-rich region of the elongating mRNA, but the exact features of the recognized sequences and how the cleaving takes place remain unknown. Rho forms a ring-shaped hexamer and advances along the mRNA, hydrolyzing ATP toward RNA polymerase (5' to 3' with respect to the mRNA). When the Rho protein reaches the RNA polymerase complex, transcription is terminated by dissociation of the RNA polymerase from the DNA.
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This bacterium is usually multiresistant to antibiotics typically prescribed for treating Gram-negative bacterial infections, including extended-spectrum beta-lactam agents (due to production by most strains of two betalactamases: one ESBL and one class B carbapenem- hydrolyzing metallolactamase), aminoglycosides, tetracycline, and chloramphenicol. Though vancomycin has been used in the past, its high Minimum inhibitory concentration (16 µg/ml) has led to a search for alternatives, especially for meningitis. Presently, ciprofloxacin, minocycline, trimethoprim-sulfamethoxazole, rifampin, and novobiocin are considered good alternatives. Most of these are classic drugs for Gram-positive bacteria and not routinely tested on Gram-negative bacteria.
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Porphyran, the major water soluble polysaccharide of Porphyra has a linear structure composed of 4-linked α-l-galactopyranose-6-sulfate (L6S) residues and 3-linked β-d- galactopyranose (G) residues. Beta porphyranase (EC 3.2.1 178; 3= Hydrolase; 3.2= Glycosylase; 3.2.1 = Glycosidases (enzymes hydrolyzing O- and S- glycosyl compounds)) acts as a glycosidase to catalyze the following chemical reaction: : Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L- galactopyranose-6-sulfate linkages in porphyran The backbone of porphyran consists largely (~70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha-L-galactopyranose-6-sulfate.
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It may also be that since ATP binding triggers NBD dimerization, the formation of the dimer may represent the "power stroke." In addition, some transporters have NBDs that do not have similar abilities in binding and hydrolyzing ATP and that the interface of the NBD dimer consists of two ATP binding pockets suggests a concurrent function of the two NBDs in the transport cycle. Some evidence to show that ATP binding is indeed the power stroke of the transport cycle was reported. It has been shown that ATP binding induces changes in the substrate-binding properties of the TMDs.
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Sodium glucuronate can be produced by the direct oxidation of starch with concentrated nitric acid. In this preparation the low availability of water keeps the starch polymers from hydrolyzing and only oxidizes the free hydroxyls, in much the same way that nitrogen dioxide would oxidize the starch. Once this reaction is complete, and the starch/nitric acid mix turns clear (after giving off nitrogen dioxide gas), the solution can be diluted, and hydrolyzed with another mineral acid. Then the oxidation is slowly quenched with sodium hydroxide (or sodium bicarbonate), forming sodium glucuronate, which can be crystallized out of solution.
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This blocks the progression of mitosis due to a prolonged activation of the microtubule in the mitotic checkpoint, resulting in cell apoptosis or reversion to the G0 phase. However, paclitaxel trevatide will effectively transport across the BBB with approximately a 100-fold higher transport rate compared to a free paclitaxel. Paclitaxel trevatide will cross the capillary medium via receptor mediated transcytosis of the low-density lipoprotein receptor-related protein 1 (LRP1) which is upregulated in some cancers. Ester hydrolyzing enzymes (esterases) then catalyze a highly stereospecific reaction that results in hydrolysis of the paclitaxel trevatide ester to carboxylic acids.
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The fungus has a number of important industrial applications because it produces the largest amounts of hydrolyzing enzymes of any thermophilic fungus. This has led to an interest in studying its genetics, and subsequently resulted in the sequencing of its genome. The proteome of T. lanuginosis contains 5100 genes, with 83 tRNA genes. One of the features that has been discovered through sequencing of the genome is that the fungus has a ubiquitin degradation pathway, which helps it respond to various environmental stressors, such as nutrient limitation, heat shock, and heavy metal exposure, and may be essential for adaptation during rising temperatures.
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Steric hindrance between the molecule neck and adjacent protofilament further inhibits full contact between protein and the microtubule and only facilitates one-dimensional diffusion along the microtubule. At this time, The protein's nucleotide binding pocket is trapped in an open state so that the structure is not hydrolyzing ATP. Once the motor reaches the end of the microtubule, the protofilament spontaneously curves itself allowing motor to make full contact with the tubulin subunit. More MCAK molecules collectively bind to the curved region supporting the theory that they do not actively peel away the microtubule but they wait patiently for it to adopt this curved conformation.
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Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolyzing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. Dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold. DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ.
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Solubilization of botryosphaeran can be enhanced through chemical derivatization with various functional groups. The influence of the composition of the nutrient medium, including nitrogen, phosphate, minerals, supplements (soybean oil, Tween 80), and the carbon source (carbohydrates),, is important in enhancing the production of botryosphaeran and biomass during fermentation by Botryosphaeria rhodina MAMB-05. Catabolite repression, and the presence of β-glucan-hydrolyzing enzymes that attack botryosphaeran during the fermentation process are critical and limit the production of botryosphaeran. Statistical factorial design methods, such as the response surface methodology (RSM), are effective in investigating complex fermentation parameters and their interactions to optimize metabolite production by microorganisms.
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This phosphorylation reaction is an equilibrium, which can be shifted by altering the proton-motive force. In the absence of a proton-motive force, the ATP synthase reaction will run from right to left, hydrolyzing ATP and pumping protons out of the matrix across the membrane. However, when the proton-motive force is high, the reaction is forced to run in the opposite direction; it proceeds from left to right, allowing protons to flow down their concentration gradient and turning ADP into ATP. Indeed, in the closely related vacuolar type H+-ATPases, the hydrolysis reaction is used to acidify cellular compartments, by pumping protons and hydrolysing ATP.
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This process depends on the stabilization of residues in the Ras switch I and switch II regions, which drives Ras into the confirmation required for enzymatic function. This interaction between Ras and neurofibromin also requires the transition state of GDP hydrolysis to be stabilized, which is performed through the insertion of the positively charged arginine finger into the Ras active site. This neutralizes the negative charges that are present on GTP during phosphoryl transfer. By hydrolyzing GTP to GDP, neurofibromin inactivates Ras and therefore negatively regulates the Ras pathway, which controls the expression of genes involved in apoptosis, the cell cycle, cell differentiation or migration.
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Proceedings of the National Academy of Sciences USA 103 (7): 24665. . PEA (N-Acylethanolamide Acid Amidase inhibitors),Solorzano C, Zhu C, Battista N, Astarita G, Lodola A, Rivara S, Mor M, Russo R, Maccarrone M, Antonietti F, Duranti A, Tontini A, Cuzzocrea S, Tarzia G, Piomelli D (2009) “Selective N-acylethanolamine- hydrolyzing acid amidase inhibition reveals a key role for endogenous palmitoylethanolamide in inflammation”. Proceedings of the National Academy of Sciences USA 106 (49): 20966-71. . and ceramide (Acid Ceramidase inhibitors).Realini N, Solorzano C, Pagliuca C, Pizzirani D, Armirotti A, Luciani R, Costi MP, Bandiera T, Piomelli D (2013) “Discovery of highly potent acid ceramidase inhibitors with in vitro tumor chemosensitizing activity”.
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In archaea such as Thermoplasma acidophilum, all the α and all the β subunits are identical, whereas eukaryotic proteasomes such as those in yeast contain seven distinct types of each subunit. In mammals, the β1, β2, and β5 subunits are catalytic; although they share a common mechanism, they have three distinct substrate specificities considered chymotrypsin-like, trypsin-like, and peptidyl-glutamyl peptide-hydrolyzing (PHGH). Alternative β forms denoted β1i, β2i, and β5i can be expressed in hematopoietic cells in response to exposure to pro-inflammatory signals such as cytokines, in particular, interferon gamma. The proteasome assembled with these alternative subunits is known as the immunoproteasome, whose substrate specificity is altered relative to the normal proteasome.
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The current dominant belief is that a "cap" of GTP is required at the ends of the ParM polymer strands to prevent them from hydrolyzing. Although GTP is hydrolyzed by the ParM units after attachment, it is believed that the energy that drives the plasmids is derived from the Gibbs free energy of the ParM monomer concentrations, and not the energy released from GTP hydrolysis. The concentrations of ParM monomer and polymer must be kept out of equilibrium at the ends where attachment is occurring for the reaction to proceed regardless of GTP concentrations. Once the ParM has pushed plasmids to opposite ends of the cell the polymer rapidly depolymerizes—returning the monomer units to the cytoplasm.
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Texture is partly a byproduct of the chemistry going on in the fermentation, which does several important things such as activate the different enzymes (protease and amylase) needed to leaven bread. Modern grain- harvesting practices have reduced the naturally occurring enzymes that grains had in former times, a result of no-longer-used grain-storage processes, so today small amounts of enzymes are routinely added to flour by manufacturers, often in the form of malted barley or sprouted grain. Proteases, dependent on their time of action and concentration levels, soften the gluten in the dough, hydrolyzing peptide bonds, increasing dough extensibility which allows the protein matrix to stretch out as the mix expands, thus leading to increased baked volumes and better structure.
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In enzymology, a N-formylglutamate deformylase () is an enzyme that catalyzes the chemical reaction :N-formyl-L-glutamate + H2O \rightleftharpoons formate + L-glutamate Thus, the two substrates of this enzyme are N-formyl-L-glutamate and H2O, whereas its two products are formate and L-glutamate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-glutamate amidohydrolase. Other names in common use include beta-citryl-L-glutamate hydrolase, formylglutamate deformylase, N-formylglutamate hydrolase, beta-citrylglutamate amidase, beta- citryl-L-glutamate amidohydrolase, beta-citryl-L-glutamate amidase, beta- citrylglutamate amidase, and beta-citryl-L-glutamate-hydrolyzing enzyme.
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Tissue transglutaminase (abbreviated as tTG or TG2) is a 78-kDa, calcium- dependent enzyme () of the protein-glutamine γ-glutamyltransferases family (or simply transglutaminase family). Like other transglutaminases, it crosslinks proteins between an ε-amino group of a lysine residue and a γ-carboxamide group of glutamine residue, creating an inter- or intramolecular bond that is highly resistant to proteolysis (protein degradation). Aside from its crosslinking function, tTG catalyzes other types of reactions including deamidation, GTP-binding/hydrolyzing, and isopeptidase activities. Unlike other members of the transglutaminase family, tTG can be found both in the intracellular and the extracellular spaces of various types of tissues and is found in many different organs including the heart, the liver, and the small intestine.
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This idea was researched extensively by Michell and his colleagues, who in 1981 were able to show that PIP2 is hydrolyzed into DAG and IP3 by a then unknown phosphodiesterase. In 1984 it was discovered that IP3 acts as a secondary messenger that is capable of traveling through the cytoplasm to the endoplasmic reticulum (ER), where it stimulates the release of calcium into the cytoplasm. Further research provided valuable information on the IP3 pathway, such as the discovery in 1986 that one of the many roles of the calcium released by IP3 is to work with DAG to activate protein kinase C (PKC). It was discovered in 1989 that phospholipase C (PLC) is the phosphodiesterase responsible for hydrolyzing PIP2 into DAG and IP3.
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Most of the ACE inhibitors on the market today are non-selective towards the two active sites of ACE because their binding to the enzyme is based mostly on the strong interaction between the zinc atom in the enzyme and the strong chelating group on the inhibitor. The resolution of the 3D structure of germinal ACE, which has only one active site that corresponds with C-domain of the somatic ACE, offers a structural framework for structure-based design approach. Although N- and C-domain have comparable rates in vitro of ACE hydrolyzing, it seems like that in vivo the C-domain is mainly responsible for regulating blood pressure. This indicates that C-domain selective inhibitors could have similar profile to that of a current non-selective inhibitors.
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The outer two rings in the stack consist of seven α subunits each, which serve as docking domains for the regulatory particles and the alpha subunits N-termini () form a gate that blocks unregulated access of substrates to the interior cavity. The inner two rings each consist of seven β subunits and in their N-termini contain the protease active sites that perform the proteolysis reactions. Three distinct catalytic activities were identified in the purified complex: chymotrypsin- like, trypsin-like and peptidylglutamyl-peptide hydrolyzing. The size of the proteasome is relatively conserved and is about 150 angstroms (Å) by 115 Å. The interior chamber is at most 53 Å wide, though the entrance can be as narrow as 13 Å, suggesting that substrate proteins must be at least partially unfolded to enter.
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It was revealed that during hypoxia phosphoinositide signaling is activated in endothelial cells, which leads to the activation of protein kinase C triggering the endocytosis of b-adrenergic receptors, which in turn leads to the cells developing insensitivity to catecholamines. During deep hypoxia and anoxia ATF- and ADF- hydrolyzing ferments disappear from the surface of endothelial cells, which leads to enhanced aggregation of platelets and endothelium hormone secretion. In the 90s, a group directed by V. A. Tkachuk published a number of papers on stretching receptors’ involvement in specific regulation of gene expression in vessel cells. It was demonstrated that when a single smooth muscle cell is rhythmically stretched, it shows increased expression of a number of genes (caldesmon, calpomin, α-actine, smooth muscle myosin), along with increased proliferation ability.
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According to the formal rules for naming inorganic compounds, the name for is aluminium acetate, though more formal names like aluminium(III) acetate and aluminium ethanoate are acceptable. The use of the "tri" multiplying prefix in the name aluminium triacetate, while not technically required, is regularly used to avoid potential confusion with related compounds with hydroxo ligands. Basic aluminium diacetate, formally hydroxyaluminium diacetate (CAS RN 142-03-0), has composition with one hydroxo ligand in place of an acetate ligand, and dibasic aluminium monoacetate, formally dihydroxyaluminium acetate (CAS RN 7360-44-3), has composition with only one acetate ligand. These three compounds are distinct in the solid phase but are usually treated as a group and described collectively as aluminium acetate in solution, due to the triacetate hydrolyzing to a mixture which includes the other two forms.
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In enzymology, an adenosylcobyric acid synthase (glutamine-hydrolysing) () is an enzyme that catalyzes the chemical reaction :4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O \rightleftharpoons 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate The four substrates of this enzyme are ATP, adenosylcobyrinic acid a,c-diamide, L-glutamine, and H2O; its four products are ADP, phosphate, adenosylcobyric acid, and L-glutamate. This enzyme belongs to the family of ligases, specifically those forming carbon- nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor (Glutamine amidotransferases). The systematic name of this enzyme class is adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase (ADP-forming). Other names in common use include CobQ, cobyric acid synthase, 5'-deoxy-5'-adenosylcobyrinic-acid-a,c-diamide:L-glutamine, amido-ligase, and Ado-cobyric acid synthase [glutamine hydrolyzing].
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Total acid hydrolysis of botryosphaeran produces only D-glucose, while partial acid hydrolysis and enzymatic hydrolysis produces a series of homologous gluco-oligosaccharides of different degrees of polymerization, which can be analyzed by High Performance Liquid Chromatography (HPLC). Enzymatic digestion of botryosphaeran under controlled conditions employing the enzymes: β-(1→3)-glucanases and β-(1→6)-glucanases from Botryosphaeria rhodina MAMB-05,Trichoderma harzianum Rifai, and Aureobasidium pullulans 1WA1, produces a mixed series of β-(1→3)- and β-(1→6)- linked gluco-oligosaccharides that can serve as prebiotics. Enzymes hydrolyzing botryosphaeran can be obtained by cultivating Botryosphaeria rhodina MAMB-05, Trichoderma harzianum Rifai and Aureobasidium pullulans 1WA1 on nutrient media containing either botryosphaeran, or the biomass derived from Botryosphaeria rhodina MAMB-05, which is a rich source of β-glucans. Prebiotics such as the (1→3)-linked gluco-oligosaccharides are emerging as nutraceuticals for inclusion in foods.
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Renin inhibitors are pharmaceutical drugs inhibiting the activity of renin that is responsible for hydrolyzing angiotensinogen to angiotensin I, which in turn reducing the formation of angiotensin II that facilitates blood pressure. Renin inhibitor is often preceded by direct, called direct renin inhibitor in order to distinguish its mechanism from other renin–angiotensin–aldosterone system-interfering drugs such as angiotensin converting enzyme inhibitors (ACEIs), angiotensin receptor blockers (ARBs) and aldosterone receptor antagonists. These drugs inhibit the first and rate-limiting step of the renin–angiotensin–aldosterone system (RAAS), namely the conversion of angiotensinogen to angiotensin I. This leads to a totality in absence of angiotensin II based on the rationale that renin only acts to inhibit this step unlike Angiotensin Converting Enzyme which is also involved in other biochemical reactions. Since the 1970s, scientists have been trying to develop potent inhibitors with acceptable oral bioavailability.
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In enzymology, a glycosylphosphatidylinositol diacylglycerol-lyase () is an enzyme that catalyzes the chemical reaction :6-(alpha-D- glucosaminyl)-1-phosphatidyl-1D-myo-inositol \rightleftharpoons 6-(alpha-D- glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol Hence, this enzyme has one substrate, 6-(alpha-D- glucosaminyl)-1-phosphatidyl-1D-myo-inositol, and two products, 6-(alpha-D- glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate and 1,2-diacyl-sn-glycerol. This enzyme belongs to the family of lyases, specifically the class of phosphorus-oxygen lyases. The systematic name of this enzyme class is 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn- glycerol-lyase [6-(alpha-D-glucosaminyl)-1D-myo-inositol 1,2-cyclic phosphate- forming]. Other names in common use include (glycosyl)phosphatidylinositol- specific phospholipase C, GPI-PLC, GPI-specific phospholipase C, VSG-lipase, glycosyl inositol phospholipid anchor-hydrolyzing enzyme, glycosylphosphatidylinositol-phospholipase C, glycosylphosphatidylinositol- specific phospholipase C, variant-surface-glycoprotein phospholipase C, 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol, and diacylglycerol- lyase (1,2-cyclic-phosphate-forming).
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