Proteolytic enzymes

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Proteolytic Enzymes

Proteolytic enzymes, also known as proteases, peptidases, or proteinases (pronunciation: pro-te-o-ly-tic en-zymes), are enzymes that catalyze proteolysis, the breakdown of proteins into smaller polypeptides or single amino acids.

Etymology

The term "proteolytic" comes from the Greek words "proteios" meaning "primary" and "lysis" meaning "loosening". The term "enzyme" is derived from the Greek words "en" meaning "in" and "zyme" meaning "leaven".

Function

Proteolytic enzymes are vital for many biological processes. They play a crucial role in digestion, where they break down protein in foods into amino acids that the body can use. They are also involved in numerous cellular processes, including cell division, immune response, and the removal of damaged proteins.

Types

There are three main types of proteolytic enzymes: serine proteases, cysteine proteases, and aspartic proteases. Each type has a different mechanism of action and is involved in different biological processes.

Serine Proteases

Serine proteases are a type of proteolytic enzyme that uses a serine residue in its active site to catalyze the hydrolysis of peptide bonds. Examples of serine proteases include trypsin, chymotrypsin, and elastase.

Cysteine Proteases

Cysteine proteases are a type of proteolytic enzyme that uses a cysteine residue in its active site to catalyze the hydrolysis of peptide bonds. Examples of cysteine proteases include cathepsins and calpains.

Aspartic Proteases

Aspartic proteases are a type of proteolytic enzyme that uses an aspartic acid residue in its active site to catalyze the hydrolysis of peptide bonds. Examples of aspartic proteases include pepsin and renin.

See Also

External links

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