Hydrolase

Hydrolase is a type of enzyme that is primarily involved in biochemical reactions that use water to break a chemical bond, a process known as hydrolysis. This class of enzymes plays a crucial role in a variety of biological processes, including digestion, metabolism, and immune response.

Structure and Function[edit | edit source]

Hydrolases are characterized by their ability to accelerate the rate of hydrolysis, a reaction in which water is used to break a chemical bond. They achieve this by lowering the activation energy required for the reaction to occur. The structure of a hydrolase enzyme is typically composed of a protein molecule, which provides a specific site, known as the active site, where the substrate can bind and undergo a chemical reaction.

Classification[edit | edit source]

Hydrolases are classified under the EC number 3 in the Enzyme Commission classification system. They are further divided into subclasses based on the type of bond they hydrolyze. Some of the major subclasses include:

EC 3.1: Esterases - enzymes that hydrolyze ester bonds.
EC 3.2: Glycosidases - enzymes that hydrolyze glycosidic bonds.
EC 3.3: Etherases - enzymes that hydrolyze ether bonds.
EC 3.4: Peptidases - enzymes that hydrolyze peptide bonds.
EC 3.5: Amidases - enzymes that hydrolyze amide bonds.
EC 3.6: Phosphatases - enzymes that hydrolyze phosphate ester bonds.

Role in Disease[edit | edit source]

Abnormalities in hydrolase function can lead to a variety of diseases. For example, deficiencies in specific hydrolases can result in lysosomal storage disease, a group of rare genetic disorders characterized by the accumulation of waste materials in cells. On the other hand, overactivity of certain hydrolases can contribute to inflammatory diseases and cancer.