Enzyme that catalyzes the hydrolysis hydrolase. Medical search. Frequent questions

They belong to the class of enzymes known as hydrolases, which catalyse the reaction of hydrolysis of various bonds with the participation of a water molecule. (stratech.co.uk)
A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. (wakehealth.edu)
2. " Hydrolases: The Most Diverse Class of Enzymes . (pediaa.com)

This gene encodes lipase A, the lysosomal acid lipase (also known as cholesterol ester hydrolase). (cancerindex.org)
We further demonstrate that combined inhibition of PDE8s and TCN 201 PDE4 significantly elevated PKA activity TCN 201 including phosphorylation of cholesterol-ester hydrolase (CEH)/hormone-sensitive lipase (HSL). (ece-inhibitor.com)

This enzyme has a preference for monounsaturated acyl chains as a substrate. (antikoerper-online.de)
Heat cannot be added to a living system, so enzymes provide an alternate pathway: they bond with a substrate (the substance involved in the chemical reaction) to form a "transition state," an unstable intermediate complex that requires less energy for the reaction to proceed. (newworldencyclopedia.org)
Only a very small portion of the enzyme, approximately ten amino acids, comes into direct contact with the substrate(s). (newworldencyclopedia.org)
This region, where the binding of the substrate(s) and the reaction occur, is known as the active site of the enzyme. (newworldencyclopedia.org)
An enzyme combines with its substrate(s) to form a short-lived enzyme-substrate complex. (newworldencyclopedia.org)
There are two models to explain how the binding of enzyme and substrate occurs: the "lock and key" model and induced fit. (newworldencyclopedia.org)
To account for the specificity of enzymes, Emil Fischer proposed that the enzyme had a particular shape into which the substrate(s) fit exactly. (newworldencyclopedia.org)
This model of exact fit, introduced in the 1890s, is often referred to as the "lock and key" model, because the enzyme binding to a substrate is analogous to the specific fit of a lock into a key. (newworldencyclopedia.org)
The active site of an enzyme can be modified as the substrate interacts with the enzyme, creating an "induced fit" between enzyme and substrate. (newworldencyclopedia.org)
3. The method of any of the preceding claims, wherein pumping equipment has been fitted to add the enzyme to the milk-based substrate while said milk-based substrate is streaming through process equipment, such as process pipes. (sumobrain.com)
The substrate binding cleft of AMY1 is composed of two aglycone and seven glycone binding subsites, of which subsite -6 (key residue: Y105) is characterized by having the highest binding affinity and being situated at the opposite end of the enzyme molecule of SBS2 at a distance of 60 Å. (dtu.dk)
As the thiolate anion is not energetically favoured in the hydrophobic interior of the enzyme, it swings into the active site where it can be stabilized by the His202 imidazolium and the dipole of helix C. The Cys123 thiolate which now lies adjacent to the acyl carbon of the substrate, is thus generated only in the presence of substrate. (inrae.fr)
The fact that some enzymes can catalyze multiple, chemically distinct, reactions exposes the weakness in our current understanding of enzyme catalysis which typically assumes that catalytic efficiency is derived from perfect optimization of an active site for a single substrate. (europa.eu)
The βLG values for the PMH-catalyzed hydrolysis of substrate classes 1-5 can be compared to the known βLG values for the uncatalyzed background reactions. (europa.eu)
To further probe the mechanism of the enzyme-catalyzed reactions, we also studied the effects of substrate structure and polarity on the enzyme catalyzed reactions. (europa.eu)
Our analysis also reveals that, surprisingly, the rates of enzymatic hydrolysis are determined more by substrate hydrophobicity than by leaving group ability or the functional group undergoing reaction. (europa.eu)
exo - and endo - refers to the ability of a glycoside hydrolase to cleave a substrate at the end (most frequently, but not always the non-reducing end) or within the middle of a chain. (cazypedia.org)
Retaining enzymes produce a product with the same stereochemistry as the glycoside substrate , and inverting enzymes give a product with the opposite stereochemistry to the glycoside substrate. (cazypedia.org)
In fact, they only catalyze the specific reactions with specific substrates as they have a very precise 3D structure and an active site to which the substrate binds. (pediaa.com)
[10] The active site of β-galactosidase catalyzes the hydrolysis of its disaccharide substrate via "shallow" (nonproductive site) and "deep" (productive site) binding. (wikidoc.org)
The goal of treatment is to reduce the rate of glucocerebroside biosynthesis so that the amount is reduced to a level that allows the residual activity of the deficient glucocerebrosidase enzyme to be more effective (substrate reduction therapy). (medscape.com)
Deficient activity of these enzymes leads to accumulation of the substrate inside neuronal lysosomes, leading to cell death. (medscape.com)

In molecular biology, glycoside hydrolase family 36 is a family of glycoside hydrolases. (wikipedia.org)
Glycoside hydrolase family 36 together with family 31 and family 27 alpha-galactosidases form the glycosyl hydrolase clan GH-D, a superfamily of alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases which are likely to share a common catalytic mechanism and structural topology. (wikipedia.org)
Glycoside hydrolase family 36 also includes enzymes with α-N-acetylgalactosaminidase EC 3.2.1.49 and stachyose synthase EC 2.4.1.67 activities. (wikipedia.org)
Glycoside hydrolase family 36 can be subdivided into 11 families, GH36A to GH36K. (wikipedia.org)
2016) Construction of the first thermostable β-glucosynthase derived from glycoside hydrolase family 3. (lu.se)

Other β-agarases belong to glycosyl hydrolase families 16 and 50, with all three groups containing a conserved glycoside hydrolase region responsible for catalysis (Fu and Kim 2010). (worthington-biochem.com)

Enzymes are essential to sustain life because most chemical reactions in biological cells , such as the digestion of food, would occur too slowly or would lead to different products without the activity of enzymes. (newworldencyclopedia.org)
Like all catalysts, enzymes work to lower the activation energy of a reaction, or the initial energy input necessary for most chemical reactions to occur. (newworldencyclopedia.org)
Enzymes may speed up reactions by a factor of many millions. (newworldencyclopedia.org)
Enzymes are usually specific, or unique, to the reactions they catalyze and the substrates that are involved in these reactions. (newworldencyclopedia.org)
These enzymes are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades (e.g., the blood-clotting cascade, the complement system, apoptosis pathways, and the invertebrate prophenoloxidase-activating cascade). (stratech.co.uk)
In support of this view, we have shown that the compound ARN077 prevents PEA and OEA hydrolysis in activated inflammatory cells and reduces tissue reactions to various proinflammatory triggers. (scienzainrete.it)
The phenomenon of catalytic promiscuity, the ability of an enzyme to catalyze reactions other than its native one, has gained significant attention in recent years as more and more promiscuous enzymes are identified. (europa.eu)
As a model enzyme, we chose to study phosphonate monoester hydrolase (PMH) which was previously shown to be highly promiscuous and which catalyzes a wide range of chemical reactions. (europa.eu)
The first phase of the project involved linear free energy relationship (LFER) analysis of the reactions that are catalyzed by the enzyme in order to gain a better understanding of the nature of the transition states for the native and promiscuous reactions. (europa.eu)
This analysis revealed that, compared to the uncatalyzed reactions, the enzyme significantly offsets the build-up of negative charge on the leaving group which is likely one of the major reasons for its catalytic efficiency. (europa.eu)
This is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. (cazypedia.org)
EC numbers do not specify enzymes, but enzyme-catalyzed reactions. (cazypedia.org)
Additionally, certain enzymes can catalyze reactions that fall in more than one class. (cazypedia.org)
Enzymes are substances that catalyze reactions by regulating the rate at which the chemical reaction proceeds without being involved in the process. (pediaa.com)
β-galactosidase can catalyze two different reactions in organisms. (wikidoc.org)
Approximately 10-15% of patients with Gaucher disease treated with imiglucerase develop antibodies to the enzyme protein, but few develop any significant allergic reactions, which are controlled with premedication with hydrocortisone, antihistamines, or both. (medscape.com)
These agents inhibit the enzyme glucosylceramide synthase, the initial enzyme in a series of reactions that result in the synthesis of most glycosphingolipids, including glucocerebroside. (medscape.com)

The encoded enzyme is able to catalyze the hydrolysis of a broad range of bioactive lipids, including those from the three main classes of fatty acid amides, N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. (antikoerper-online.de)
The acyl-enzyme is stabilized by hydrogen bonding from the amide backbone of 'oxyanion hole' residues, consistent with formation of a tetrahedral oxyanion during nucleophilic attack by Ser112. (rcsb.org)
Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (lookformedical.com)
Lipases are triacylglycerol acyl hydrolases with the enzyme number EC 3.1.1.3. (edu.ng)
Lipases (triacylglycerol acyl hydrolases, E.C. 3.1.1.3), are a family of enzymes that catalyzetheconversion of triacylglycerol to glycerol and fatty acids. (edu.ng)

This gene encodes a fatty acid amide hydrolase that shares a conserved protein motif with the amidase signature family of enzymes. (antikoerper-online.de)
For instance, many household cleaners use enzymes to speed up the breakdown of protein or starch stains on clothes. (newworldencyclopedia.org)
Both PI3K inhibitor (medical drug that functions by inhibiting one or more of the phosphoinositide 3-kinase enzymes) and over-expression of sortilin 1 protein. (mmpc.org)
A protease is an enzyme that conducts proteolysis, i.e., the protein catabolism by hydrolysis of the peptide bonds that link amino acids together in the polypeptide chain which form the protein. (stratech.co.uk)
In a search for plant homologues of dipeptidyl peptidase III (DPP III) family, we found a predicted protein from the moss Physcomitrella patens (UniProt entry: A9TLP4), which shared 61% sequence identity with the Arabidopsis thaliana uncharacterized protein, designated Nudix hydrolase 3. (irb.hr)
Both proteins contained all conserved regions of the DPP III family, but instead of the characteristic hexapeptide HEXXGH zinc-binding motif, they possessed a pentapeptide HEXXH, and at the N-terminus, a Nudix box, a hallmark of Nudix hydrolases, known to act upon a variety of nucleoside diphosphate derivatives.To investigate their biochemical properties, we expressed heterologously and purified Physcomitrella (PpND) and Arabidopsis (AtND) protein. (irb.hr)

Based on catalytic domain similarities, β-Agarase II of Pseudoalteromonas atlantica has been designated part of the glycosyl hydrolase 86 (GH86) family. (worthington-biochem.com)
Most enzymes are proteins , though certain nucleic acids , called ribozymes , are also capable of catalytic activity. (newworldencyclopedia.org)
The amino acids side chains that make up the active site are molded into a precise shape, which enables the enzyme to perform its catalytic function. (newworldencyclopedia.org)
The chloride-binding functions to activate the enzyme, which acts by a two-step mechanism involving a catalytic nucleophile base (usually an Asp) and a catalytic proton donor (usually a Glu) that are responsible for the formation of the beta-linked glycosyl-enzyme intermediate. (embl.de)
The orange-colored catalytic intermediate, ES(red), previously detected in the wild-type enzyme and proposed herein to be a carbanion, was not observed during hydrolysis by H265Q. (rcsb.org)
While the updated catalytic mechanism shares features with the serine proteases, MCP hydrolase-specific chemistry highlights the versatility of the Ser-His-Asp triad. (rcsb.org)
Many raw starch-degrading enzymes contain secondary carbohydrate binding sites on the catalytic domain or on separate starch binding domains. (dtu.dk)
The Cys-His-Asp catalytic triad found in dienelactone hydrolase (DLH) is unusual for several reasons. (inrae.fr)
Analysis of the crystal structure of the enzyme allowed us to identify several key catalytic residues in the active site. (europa.eu)
The above referred to acetylation response stage (oximolysis) certainly mimics just LTBP1 the initial stage from the catalytic procedure for the serine hydrolases, such as for example AcChE, however the full enzyme catalyzed procedure contains two successive levels, deacetylation and acetylation, that's, hydrolysis of seryl-acetyl-ester shaped in energetic site from the AcChE [25]. (buyresearchchemicalss.net)
Let's assume that oximate promotes the hydrolysis of AcSCh+ performing as pseudo-hydrolase/thioesterase, additional investigation from the destiny of pyridinium-4-oxime-ester (acetylated oxime) was essential to offer mechanistic top features of the next, deacetylation, stage of the full total catalytic procedure. (buyresearchchemicalss.net)

This multiunctional enzyme catalyzes both the synthesis and CC hydrolysis of cyclic ADP-ribose, a calcium messenger that can CC mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to CC regulate a wide range of physiological processes. (expasy.org)
They catalyze the hydrolysis and the synthesis of esters formed from glycerol and long-chain fatty acids. (edu.ng)

are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. (wikipedia.org)
Glycoside hydrolases are enzymes that catalyze the hydrolysis of the glycosidic linkage of glycosides, leading to the formation of a sugar hemiacetal or hemiketal and the corresponding free aglycon. (cazypedia.org)
β-galactosidase , also called lactase , beta-gal or β-gal , is a glycoside hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides through the breaking of a glycosidic bond . (wikidoc.org)

They belong to the class of serine hydrolases and do not require any cofactor. (edu.ng)

A metallocarboxypeptidase that is predominantly expressed as a membrane-bound enzyme. (nih.gov)

The computational evaluation of HOC-assisted AcSCh+ hydrolysis recommended the concerted system using the kinetic hurdle (= 0.1 M. Oximolysis Response Ester Nucleophile = 0.1 M and 25 C (Body S5). (buyresearchchemicalss.net)
Antimicrobial lipids inhibit S. aureus growth and induce the staphylococcal proteolytic cascade, producing aureolysin (Aur) which processes the lipase glycerol ester hydrolase (Geh). (uwo.ca)

Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate the mature lysosomal enzyme. (thermofisher.com)
It is a lysosomal enzyme and used as a long-term enzyme replacement therapy in patients with a confirmed diagnosis of Fabry disease. (assaygenie.com)

Beta Galactosidase encodes a member of the glycosyl hydrolase 35 family of proteins. (thermofisher.com)
Enzymes (and other proteins) are composed of amino acid chains called polypeptide chains. (newworldencyclopedia.org)
Proteases determine the lifetime of other proteins playing an important physiological role like hormones, antibodies, or other enzymes-this is one of the fastest "switching on" and "switching off" regulatory mechanisms in the physiology of an organism. (stratech.co.uk)
Hydrolases are involved in the breakdown of complex macromolecules such as proteins, nucleic acids, and carbohydrates. (pediaa.com)
More recently, the concept of lysosomal storage disease has been expanded to include deficiencies or defects in proteins necessary for the normal post-translational modification of lysosomal enzymes (which themselves are often glycoproteins), activator proteins, or proteins important for proper intracellular trafficking between the lysosome and other intracellular compartments. (medscape.com)

Meta-cleavage product (MCP) hydrolases are members of the α/β-hydrolase superfamily that utilize a Ser-His-Asp triad to catalyze the hydrolysis of a C-C bond. (rcsb.org)
The overall goal of this project was to use the tools of physical organic chemistry to probe the mechanistic features of promiscuous enzymes in the alkaline phosphatase superfamily, a structurally related family of enzymes that appears to be particularly prone to promiscuous behaviour. (europa.eu)

For example, lactose intolerance, the inability to digest significant amounts of lactose, which is the major sugar found in milk , is caused by a shortage of the enzyme lactase. (newworldencyclopedia.org)
A few are evolved beta-galactosidase (EBG), beta-glucosidase , 6-phospho-beta-galactosidase, beta-mannosidase, and lactase-phlorizin hydrolase. (wikidoc.org)
Many adult humans lack the lactase enzyme, which has the same function of beta-gal, so they are not able to properly digest dairy products. (wikidoc.org)

Hydrolytic lysosomal glucocerebroside-specific enzyme indicated for long-term enzyme replacement therapy for type 1 Gaucher disease. (medscape.com)

Chronically high levels of succinylacetone are associated with tyrosinemia type I. Type I tyrosinemia is an inherited metabolism disorder due to a shortage of the enzyme fumarylacetoacetate hydrolase that is needed to break down tyrosine. (hmdb.ca)

Lipases (E.C. 3.1.1.3) are hydrolytic enzymes with biotechnological potentials. (edu.ng)
Examples of hydrolases are proteases and lipases, while examples of lyases are decarboxylases and aldolases. (pediaa.com)

The AZ 3146 kinase activity assay mechanistic research also will abide by the stepwise response mechanism recommended for natural formylthiocholine hydrolysis [20,21] and Formula (6) provides kinetic hurdle, = 99.3 kJ?mol?1. (buyresearchchemicalss.net)
Analogous towards the mechanism from the AChE-catalyzed procedure, the oxime-mediated AcSCh+ hydrolysis includes two successive stagesfirst, the oximolysis, that's, the acetylation stage seen as a the stepwise system (Body 4a) and second, the deacetylation stage, seen as a the concerted HO? (buyresearchchemicalss.net)

Proteases, also known as peptidases or proteolytic enzymes, are a large group of enzymes. (stratech.co.uk)
It has not been observed in other hydrolytic enzymes and it is virtually inactive when it is produced by site-directed mutagenesis in the proteases. (inrae.fr)

Here, we show that URB597, a selective inhibitor of the enzyme fatty-acid amide hydrolase, which catalyzes the intracellular hydrolysis of the endocannabinoid anandamide, exerts potent antidepressant-like effects in the mouse tail-suspension test and the rat forced-swim test. (erowid.org)
The actions of these lipid messengers are terminated by enzyme-mediated hydrolysis, which is catalyzed by 2 intracellular lipid amidases: N-acylethanolamine acid amidase (NAAA) and fatty acid amide hydrolase (FAAH). (scienzainrete.it)
The latter response is reversed by pharmacological blockade of NAAA-mediated FAE hydrolysis, suggesting that inhibition of intracellular NAAA activity might represent a novel mechanistic approach to control inflammation. (scienzainrete.it)

Raffinose synthase EC 2.4.1.82 is the key enzyme that channels sucrose into the raffinose oligosaccharide pathway. (wikipedia.org)
BphD, the MCP hydrolase from the biphenyl degradation pathway, hydrolyzes 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to 2-hydroxypenta-2,4-dienoic acid (HPD) and benzoate. (rcsb.org)
Dienelactone hydrolases play a crucial role in chlorocatechol degradation via the modified ortho cleavage pathway. (inrae.fr)
Dienelactone hydrolase (DLH), an enzyme from the beta-ketoadipate pathway, catalyzes the hydrolysis of dienelactone to maleylacetate. (inrae.fr)
The root-mean-square deviation from ideal bond distances for the model is 0.014 A and the error in atomic co-ordinates is estimated to be 0.15 A. DLH is a monomeric enzyme containing 236 amino acid residues and is a member of the beta-ketoadipate pathway found in bacteria and fungi. (inrae.fr)

Catalyzes hydrolytic cleavage of glucocerebroside (a glycoprotein) to glucose and ceramide within the lysosomes of phagocytic cells in the reticuloendothelial system. (medscape.com)

It is a complex process promoted by the interaction of many groups of microorganisms and has four major steps: hydrolysis, acidogenesis, acetogenesis, and methanogenesis. (intechopen.com)
The β-glucosidase enzymes are widespread in microorganisms, and their genes of production can differ in strains of the same species [ 9 ]. (springeropen.com)
The research focus is within the area "enzymes of extremophilic microorganisms", especially concerning thermostable glycoside hydrolases (including representatives from GH-family 1, 3, 10, 12 and 13). (lu.se)

An enzyme is a biological catalyst that regulates the rate of a chemical reaction in a living organism. (newworldencyclopedia.org)

Retaining and inverting classification refers to the stereochemical outcome of the hydrolysis reaction catalyzed by the glycoside hydrolase. (cazypedia.org)
The hydrolysis reaction catalyzed by hydrolases involves the addition of a water molecule to the bond that is to be broken. (pediaa.com)

They play important roles in the hydrolysis of triglycerides to free fatty acids and glycerol as commercial biocatalysts. (edu.ng)

This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes. (wikipedia.org)
The carbohydrate-active enzymes database (CAZy", NUCLEIC ACIDS RES. (sumobrain.com)

This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. (unl.edu)

If different enzymes (for instance from different organisms) catalyze the same reaction, then they receive the same EC number. (cazypedia.org)
Enzymes regulate most biological processes that happen within living organisms. (pediaa.com)

The findings support a role for anandamide in mood regulation and point to fatty-acid amide hydrolase as a previously uncharacterized target for antidepressant drugs. (erowid.org)

Finally we showed that optimal growth in trilinolein requires Aur, and might reflect a requirement for the proGeh form of the enzyme to convert trilinolein into toxic linoleic acid, despite that fact that both unprocessed and processed Geh catalyze the hydrolysis of trilinolein. (uwo.ca)
Enzyme replacement therapy (ERT) with glucocerebrosidase purified from human placenta was FDA approved in 1991, followed by approval in 1994 of a recombinant form of the enzyme produced in cultured Chinese hamster ovary (CHO) cells, marketed as imiglucerase (Cerezyme). (medscape.com)

Glycoside hydrolases are also referred to as glycosidases. (cazypedia.org)

A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. (wikipedia.org)
A necessary consequence of the EC classification scheme is that codes can be applied only to enzymes for which a function has been biochemically identified. (cazypedia.org)

Alpha-amylase is an essential enzyme in alpha-glucan metabolism, acting to catalyse the hydrolysis of alpha-1,4-glucosidic bonds of glycogen, starch and related polysaccharides. (embl.de)
3.2.1.1) catalyzes the hydrolysis of internal 1,4-α-D-glucosidic bonds in starch and related polysaccharides. (dtu.dk)
The main difference between hydrolases and lyases is that hydrolases catalyze the hydrolysis of chemical bonds using water molecules, whereas lyases catalyze the cleavage of chemical bonds without the use of water molecules. (pediaa.com)
Hydrolases are a type of enzyme that use water to break chemical bonds. (pediaa.com)
Lyases are a type of enzyme that catalyzes the breakdown of various chemical bonds without the use of water. (pediaa.com)
They catalyze the formation of carbon-carbon bonds by joining two carbonyl compounds. (pediaa.com)
Hydrolases catalyze the hydrolysis of chemical bonds using water molecules, whereas lyases catalyze the cleavage of chemical bonds without the use of water molecules. (pediaa.com)

It is an essential enzyme in the human body. (wikidoc.org)

Glycoside hydrolases can catalyze the hydrolysis of O-, N- and S-linked glycosides. (cazypedia.org)
5. Rather, MY, Nordberg Karlsson E, Adlercreutz P. ( 2015 ) Complexation of alkyl glycosides with α-cyclodextrin can have drastically different effects on their conversion by glycoside hydrolases. (lu.se)

This enzyme functions in the lysosome to catalyze the hydrolysis of cholesteryl esters and triglycerides. (cancerindex.org)

Searching for the presence and activity of the enzymes as well as linking structure and function of microbial communities allows to develop a fundamental understanding of the processes, leading to methane production. (intechopen.com)
Microbial Enzymes and Their Mechanisms in the Bioremediation of Pollutants. (igi-global.com)
Microbial enzymes have a wide range of metabolic activities and are involved in the transformation of pollutants. (igi-global.com)

We then confirmed that geh was required for lipase activity and both forms of the purified enzyme had lipase activity. (uwo.ca)

This is the first report of a dual activity enzyme, highly conserved in land plants, which catalyzes the hydrolysis of a peptide bond and of a phosphate bond, acting both as a dipeptidyl peptidase III and an atypical Nudix hydrolase. (irb.hr)

Catalyzes the hydrolysis of pteroylpolyglutamic acids in gamma linkage to pterolylmonoglutamic acid and free glutamic acid. (bvsalud.org)

Alpha-amylase is classified as family 13 of the glycosyl hydrolases and is present in archaea, bacteria, plants and animals. (embl.de)
Glycosyl hydrolases family 35. (unl.edu)
Galactosidase A is a homodimeric glycoprotein that belongs to the glycosyl hydrolase 27 family. (assaygenie.com)

Alpha-galactosidase (EC 3.2.1.22) (melibiase) catalyzes the hydrolysis of melibiose into galactose and glucose. (wikipedia.org)
galactosyl moieties from glycolipids and glycoproteins and catalyze the hydrolysis of melibiose into galactose and glucose. (assaygenie.com)
Oleuropein, the main bitter phenolic glucoside responsible for green olive bitterness, may be degraded by the β-glucosidase enzyme to release glucose and phenolic compounds. (springeropen.com)
It catalyzes the hydrolysis of glucocerebroside to glucose and ceramide, which results in reduced spleen and liver enlargement and increased RBCs and platelets. (medscape.com)

The studies involve biochemical structure/function-related studies of enzymes with a biotechnological potential. (lu.se)

Lysosomal storage disorders (LSDs) are caused by a genetic deficiency in the enzymatic function of the hydrolases stored within lysosomes, causing an accumulation of materials meant for degradation. (medscape.com)

This enzyme catalyzes the hydrolysis of a terminal beta-linked galactose residue from ganglioside substrates and other glycoconjugates. (thermofisher.com)
Beta-galactose is used in such dairy products as yogurt, sour cream, and some cheeses which are treated with the enzyme to break down any lactose before human consumption. (wikidoc.org)

The degradation of insoluble polysaccharides by glycoside hydrolases is relative inefficient as the polysaccharide chains often are barely inaccessible to the active site of the enzymes. (dtu.dk)

Agricultural residues can thus be used for the production of various value-added products, such as industrially important enzymes. (mdpi.com)
Our aim was to gain a better understanding of the origins of promiscuity and, ultimately, to use this information as a guide for the rational design of new enzymes with industrially useful functions. (europa.eu)

Classically, lysosomal storage diseases encompassed only enzyme deficiencies of the lysosomal hydrolases. (medscape.com)

Protease-catalyzed hydrolysis relieves its quenching effect, yielding brightly fluorescent dye-labeled short peptides. (stratech.co.uk)

Alpha-N-acetylgalactosaminidase (EC 3.2.1.49) catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D- galactosaminides. (wikipedia.org)
The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. (unl.edu)

Enzymes can be affected by molecules that increase their activity (activators) or decrease their activity (inhibitors). (newworldencyclopedia.org)
By inhibiting the activity of these enzymes, aspirin suppresses our experience of pain and inflammation. (newworldencyclopedia.org)
Color intensity is not an indication of enzyme activity. (sunsonenzymes.com)
The known activities of PMH include the hydrolysis of phosphate mono-, di-, and triesters (1,2,3 respectively), sulfate monoesters (5), and sulfonate monoesters (6) in addition to its native activity towards the hydrolysis of phosphonate monoesters (4). (europa.eu)
However, the β-glucosidase was activated with an increase of NaCl concentration, with a maximum activity obtained at 8% NaCl (w/v). The enzyme activity was optimal at pH 5 for both strains, while the optimum temperature was 45 °C for L. plantarum FSO1 and 35 °C for C. pelliculosa L18. (springeropen.com)
A few patients with Gaucher disease have developed antibodies that impair enzyme activity. (medscape.com)

Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). (wikipedia.org)

AMY1 is so far the simplest enzyme known to possess two distinct carbohydrate surface binding sites (here called starch binding site 1 and 2, in short: SBS1 and SBS2). (dtu.dk)

Bioremediation is the process, with the help of microbes or their enzymes, to remove the pollutants present in the environment and change them into non-toxic compounds. (igi-global.com)

Starch sugar is the sugar produced by starch as the raw material and the enzyme preparation is widely used in the preduction of starch sugar. (sunsonenzymes.com)

It catalyzes the hydrolysis of an unsubstituted, C-terminal glutamyl residue, typically from PTEROYLPOLYGLUTAMIC ACIDS . (nih.gov)

Enzymes induced in 4-fluorobenzoate-utilizing bacteria have been classified into three groups on the basis of their specificity towards cis- and trans-dienelactone. (inrae.fr)

Anatomy13

Organisms15

Chemicals and Drugs155

Analytical, Diagnostic and Therapeutic Techniques and Equipment24

Phenomena and Processes44

Disciplines and Occupations1

Technology, Industry, Agriculture1

Information Science5

Health Care3

Class of enzymes3

Cholesterol ester hydrolase2

Substrate22

Glycoside Hydrolase Family5

Glycosyl hydrolase families1

Reactions17

Acyl5

Protein6

Catalytic11

Synthesis2

Glycosidic3

Serine hydrolases1

Membrane-bound1

Ester2

Lysosomal enzyme2

Proteins5

Superfamily2

Lactase3

Long-term enzyme replace1

Shortage of the enzyme1

Lipases2

Mechanism2

Proteases2

Intracellular3

Pathway5

Hydrolytic1

Microorganisms3

Living organism1

Reaction catalyzed2

Glycerol1

CAZy2

Beta-galactosidase1

Organisms2

Fatty1

Form of the enzyme2

Glycosidases1

Classification2

Bonds7

Essential enzyme1

Glycosides2

Triglycerides1

Microbial3

Lipase activity1

Peptide1

Acid1

Family3

Glucose4

Biotechnological1

Enzymatic1

Galactose2

Polysaccharides1

Industrially2

Deficiencies1

Protease1

Residues2

Activity6

CAZypedia1

Carbohydrate1

Compounds1

Starch1

Terminal1

Specificity1