Hydrolase

In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond:

${\displaystyle {\ce {A-B + H2O}}\quad {\xrightarrow[{\text{ hydrolase }}]{}}\quad {\ce {A-OH + B-H}}}$

This typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases.

Esterases cleave ester bonds in lipids and phosphatases cleave phosphate groups off molecules. An example of crucial esterase is acetylcholine esterase, which assists in transforming the neuron impulse into the acetate group after the hydrolase breaks the acetylcholine into choline and acetic acid.[1] Acetic acid is an important metabolite in the body and a critical intermediate for other reactions such as glycolysis. Lipases hydrolyze glycerides. Glycosidases cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds. Nucleosidases hydrolyze the bonds of nucleotides.[2]

Hydrolase enzymes are important for the body because they have degradative properties. In lipids, lipases contribute to the breakdown of fats and lipoproteins and other larger molecules into smaller molecules like fatty acids and glycerol. Fatty acids and other small molecules are used for synthesis and as a source of energy.[1]