Hydrolase

Hydrolases are enzymes that catalyze the hydrolysis of a range of bonds. They frequently show broad specificity, and this characteristic has posed problems in naming them. The systematic name for an enzyme that performs a hydrolytic reaction includes the term hydrolase, whereas the trivial name is formed by the addition of the suffix ase to the name of the substrate or the class of substrate on which the enzyme acts. Those hydrolases that act on carboxylic esters, thiolesters, phosphomonoesters, phosphodiesters, phosphotriesters, diphosphomonoesters, DNA and RNA have been classified as a group that acts on ester bonds. The glycosidases hydrolyze O-glycosyl, N-glycosyl, and S-glycosyl compounds; etherases act on ether and thioether bonds; peptidases hydrolyze aminoacylpeptide, dipeptide, and dipeptidylpeptide bonds. Other categories of hydrolase are the serine carboxypeptidases and serine proteinases, which contain a DIFP (diisopropyl fluorophosphate)-sensitive a serine residue at their active sites, the thiol proteinases, the carboxyl proteinases, and the metalloproteinases There are also hydrolases that act on C—N , rather than peptide, bonds, and the substrates for these enzymes include amides, cyclic amides, linear amidines, cyclic amidines, and nitriles. Other hydrolases act on acid anhydrides and C—C , halide, P—N , S—N , and C—P bonds.

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