EC 126.96.36.199 - Trypsin
IntEnz Enzyme Nomenclature
sperm receptor hydrolase
- Preferential cleavage: Arg┼, Lys┼.
The single polypeptide chain cattle β-trypsin is formed from trypsinogen by cleavage of one peptide bond. Further peptide bond cleavages produce α and other iso-forms. Isolated as multiple cationic and anionic trypsins  from the pancreas of many vertebrates and from lower species including crayfish, insects (cocoonase) and microorganisms (Streptomyces griseus) . Type example of peptidase family S1. Formerly EC 188.8.131.52.
Links to other databases
Structural basis of the activation and action of trypsin.Acc. Chem. Res. 11: 114-122 (1978).
Trypsinogens and trypsins of various species.Methods Enzymol. 19: 41-63 (1970).
Critical evaluation of comparative model building of Streptomyces griseus trypsin.Biochemistry 23: 6570-6575 (1984). [PMID: 6442164]
Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin.Eur. J. Biochem. 163: 303-312 (1987). [PMID: 3643848]
Isolation and characterization of a cDNA encoding rat cationic trypsinogen.Biochemistry 26: 3081-3086 (1987). [PMID: 3607011]
Structure and function of serine proteases.In: Neuberger, A. and Brocklehurst, K. (Eds.)
New Comprehensive Biochemistryvol. 16, Elsevier, Amsterdam, 1987, 159-200
Nucleotide sequence of the human pancreatic trypsinogen III cDNA.Nucleic Acids Res. 18: 1631 (1990). [PMID: 2326201]
[EC 184.108.40.206 created 1961 as EC 220.127.116.11, transferred 1972 to EC 18.104.22.168]