Cysteine protease
Cysteine Protease
Cysteine protease (pronounced: sis-teen pro-tease) is a type of protease containing a cysteine residue that is essential to its catalytic function.
Etymology
The term "Cysteine protease" is derived from the amino acid cysteine, which plays a crucial role in its function, and "protease", a type of enzyme that conducts proteolysis - the breakdown of proteins into smaller polypeptides or single amino acids.
Function
Cysteine proteases have a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic dyad or triad. These enzymes are involved in numerous physiological and pathological processes, including protein synthesis, cell growth and apoptosis, antigen presentation, and pro-inflammatory responses.
Classification
Cysteine proteases are classified into clans and families. Clans are groups of families for which there is evidence of common ancestry based on structural and functional similarities. Families are groups of proteases that have similar amino acid sequences. The two main clans of cysteine proteases are the CA clan (papain family) and the CD clan (caspase family).
Related Terms
- Protease: An enzyme that conducts proteolysis, protein catabolism by hydrolysis of peptide bonds.
- Cysteine: A semi-essential proteinogenic amino acid.
- Proteolysis: The breakdown of proteins into smaller polypeptides or single amino acids.
- CA clan: A clan of cysteine proteases that includes the papain family.
- CD clan: A clan of cysteine proteases that includes the caspase family.
External links
- Medical encyclopedia article on Cysteine protease
- Wikipedia's article - Cysteine protease
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