Hydrolases


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Related to Hydrolases: Isomerases, Ligases, Lyases, Acid hydrolases

Hydrolases

 

a class of enzymes that catalyze reactions of hydrolytic decomposition (with the participation of water) of intramolecular bonds (hydrolysis). Hydrolases are widespread in plant and animal cells. They participate in processes of metabolism of proteins, nucleic acids, carbohydrates, lipids, and other biologically important substances. Depending on the type of bond hydrolyzed, hydrolases are divided into a number of subclasses: hydrolases acting on ester bonds (for example, lipase), glucoside bonds (amylase), peptide bonds (pepsin), and acid-anhydride bonds (adenosine triphosphatase).

By their chemical nature, most hydrolases are simple proteins. The presence of unaltered sulfhydryl groups (SH—) with a definite place in the polypeptide chain is necessary for the appearance of their catalytic activity. A number of hydrolases are produced in crystalline form (urease, pepsin, trypsin, and chymotrypsin). The mechanism of the catalytic action of some hydrolases that have been studied includes the addition of an enzyme, with decomposition of the substance followed by splitting off of the reaction products and liberation of the enzyme. It has been shown that in the mechanisms of enzymatic hydrolysis there is much in common with the action mechanism of transferase and that some hydrolases can transfer the groups being split off not only to water but also to other molecules.

E. I. KOROLEV

References in periodicals archive ?
Screening and separation of industrially useful hydrolases from the wasteful skim latex serum of Hevea brasiliensis, The 4th ICCBE in Conjunction with The 26th Symposium of MCE, UMS, Sabah, pp: 799-808.
Hydrophilic domains of scaffolding protein CbpA promote glycosyl hydrolase activity and localization of cellulosomes to the cell surface of Clostridium cellulovorans.
The heart of the system, known as activity-based protein profiling, is a chemical probe that binds to glycoside hydrolases and gives off information indicating just how active each of those enzymes is moment by moment.
The large family of serine hydrolases are largely underexplored as drug targets.
In initial tests using recently advanced techniques for measuring enzyme-inhibition strength and specificity, the Scripps Research scientists found that molecules known as 1,2,3-triazole ureas could powerfully inhibit some serine hydrolases without affecting other enzymes.
High-throughput substrate profiling of hydrolases and proteases is covered in good detail; included are the use of solution assays, solid support-based screening, and chip-based assays.
This material contains enzymes such as hydrolases, de-Esterases, reductiveases, and oxidases which are said to promote the conversion of a wide range of malodorous substances to their heavier molecule weight, non-odorous salt forms.
for which humans do not express suitable hydrolases.
The enzymes currently in use are mostly hydrolases.
Activity-based protein profiling: the serine hydrolases.
Almac is providing a diverse, A-Z range of enzymes including reductases, transaminases, hydrolases, nitrilases and many others.
the clan GH-H of glycoside hydrolyses, is the largest family of glycoside hydrolases, transferases and isomerases comprising nearly 30 different enzyme specificities.