Cysteine protease
Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad.
Cysteine peptidase, CA clan | |||||||||
---|---|---|---|---|---|---|---|---|---|
Crystal structure of the cysteine peptidase papain in complex with its covalent inhibitor E-64. Rendered from PDB: 1PE6 | |||||||||
Identifiers | |||||||||
Symbol | Peptidase_C1 | ||||||||
Pfam | PF00112 | ||||||||
Pfam clan | CL0125 | ||||||||
InterPro | IPR000668 | ||||||||
SMART | SM00645 | ||||||||
PROSITE | PDOC00126 | ||||||||
MEROPS | C1 | ||||||||
SCOP2 | 1aec / SCOPe / SUPFAM | ||||||||
OPM superfamily | 355 | ||||||||
OPM protein | 1m6d | ||||||||
|
Discovered by Gopal Chunder Roy in 1873, the first cysteine protease to be isolated and characterized was papain, obtained from Carica papaya. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe. In fact, the latex of dozens of different plant families are known to contain cysteine proteases. Cysteine proteases are used as an ingredient in meat tenderizers.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.