Hydrolase

Not to be confused with hydroxylase.

In biochemistry, a hydrolase or hydrolytic enzyme is an enzyme that catalyzes the hydrolysis of a chemical bond. For example, an enzyme that catalyzed the following reaction is a hydrolase:

A–B + H₂O → A–OH + B–H

Nomenclature

Systematic names of hydrolases are formed as "substrate hydrolase." However, common names are typically in the form "substratease." For example, a nuclease is a hydrolase that cleaves nucleic acids.

Classification

Hydrolases are classified as EC 3 in the EC number classification of enzymes. Hydrolases can be further classified into several subclasses, based upon the bonds they act upon:

• EC 3.1: ester bonds (esterases: nucleases, phosphodiesterases, lipase, phosphatase)
• EC 3.2: sugars (DNA glycosylases, glycoside hydrolase)
• EC 3.3: ether bonds
• EC 3.4: peptide bonds (Proteases/peptidases)
• EC 3.5: carbon-nitrogen bonds, other than peptide bonds
• EC 3.6 acid anhydrides (acid anhydride hydrolases, including helicases and GTPase)
• EC 3.7 carbon-carbon bonds
• EC 3.8 halide bonds
• EC 3.9: phosphorus-nitrogen bonds
• EC 3.10: sulphur-nitrogen bonds
• EC 3.11: carbon-phosphorus bonds
• EC 3.12: sulfur-sulfur bonds
• EC 3.13: carbon-sulfur bonds

Clinical considerations

Hydrolase secreted by Lactobacillus jensenii in the human gut stimulates the liver to secrete bile salts that aids in the digestion of food.

Etymology and pronunciation

The word hydrolase (/ˈhaɪdroʊleɪs, -leɪz/) suffixes the combining form of -ase to the hydrol syllables of hydrolysis.

See also

• Phosphorylase
• Serine hydrolase

References

• EC 3 Introduction from the Department of Chemistry at Queen Mary, University of London, only covers 3.1-3.4
• More detailed taxonomy