Back كيموتربسين Arabic Quimotripsina Catalan Chymotrypsin Czech Chymotrypsin B German Quimotripsina Spanish Kümotrüpsiin Estonian کیموتریپسین Persian Kymotrypsiini Finnish Chymotrypsine French Quimotripsina Galician
| Chymotrypsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystallographic structure of Bos taurus chymotrypsinogen[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 3.4.21.1 | ||||||||
| CAS no. | 9004-07-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Chymotrypsin C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.2 | ||||||||
| CAS no. | 9036-09-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Chymotrypsin (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum, where it performs proteolysis, the breakdown of proteins and polypeptides.[2] Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine).[3] These amino acids contain an aromatic ring in their side chain that fits into a hydrophobic pocket (the S1 position) of the enzyme. It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P1 side chain and the enzyme S1 binding cavity accounts for the substrate specificity of this enzyme.[4][5] Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine at the P1 position.[6]
Structurally, it is the archetypal structure for its superfamily, the PA clan of proteases.
- ^ PDB: 1CHG; Freer ST, Kraut J, Robertus JD, Wright HT, Xuong NH (April 1970). "Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation". Biochemistry. 9 (9): 1997–2009. doi:10.1021/bi00811a022. PMID 5442169.
- ^ Wilcox PE (1970). "[5] Chymotrypsinogens—chymotrypsins". Chymotrypsinogens — chymotrypsins. Methods in Enzymology. Vol. 19. pp. 64–108. doi:10.1016/0076-6879(70)19007-0. ISBN 978-0-12-181881-4.
- ^ Cotten, Steven W. (2020-01-01), Clarke, William; Marzinke, Mark A. (eds.), "Chapter 33 - Evaluation of exocrine pancreatic function", Contemporary Practice in Clinical Chemistry (Fourth Edition), Academic Press, pp. 573–585, ISBN 978-0-12-815499-1, retrieved 2023-03-18
- ^ Appel W (December 1986). "Chymotrypsin: molecular and catalytic properties". Clin. Biochem. 19 (6): 317–22. doi:10.1016/S0009-9120(86)80002-9. PMID 3555886.
- ^ Berger A, Schechter I (February 1970). "Mapping the active site of papain with the aid of peptide substrates and inhibitors". Philos. Trans. R. Soc. Lond. B Biol. Sci. 257 (813): 249–64. Bibcode:1970RSPTB.257..249B. doi:10.1098/rstb.1970.0024. PMID 4399049. S2CID 6877875.
- ^ Cotten, Steven W. (2020-01-01), Clarke, William; Marzinke, Mark A. (eds.), "Chapter 33 - Evaluation of exocrine pancreatic function", Contemporary Practice in Clinical Chemistry (Fourth Edition), Academic Press, pp. 573–585, ISBN 978-0-12-815499-1, retrieved 2023-03-18