The Enzyme Database

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Accepted name: trypsin
Reaction: Preferential cleavage: Arg┼, Lys┼
Other name(s): α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase
Comments: 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 [5] from the pancreas of many vertebrates and from lower species including crayfish, insects (cocoonase) and microorganisms (Streptomyces griseus) [3]. Type example of peptidase family S1.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9002-07-7
1.  Huber, R. and Bode, W. Structural basis of the activation and action of trypsin. Acc. Chem. Res. 11 (1978) 114–122.
2.  Walsh, K.A. Trypsinogens and trypsins of various species. Methods Enzymol. 19 (1970) 41–63.
3.  Read, R.J., Brayer, G.D., Jurásek, L. and James, M.N.G. Critical evaluation of comparative model building of Streptomyces griseus trypsin. Biochemistry 23 (1984) 6570–6575. [PMID: 6442164]
4.  Fiedler, F. Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin. Eur. J. Biochem. 163 (1987) 303–312. [DOI] [PMID: 3643848]
5.  Fletcher, T.S., Alhadeff, M., Craik, C.S. and Largman, C. Isolation and characterization of a cDNA encoding rat cationic trypsinogen. Biochemistry 26 (1987) 3081–3086. [PMID: 3112218]
6.  Polgár, L. Structure and function of serine proteases. In: Neuberger, A. and Brocklehurst, K. (Ed.), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, pp. 159–200.
7.  Tani, T., Kawashima, I., Mita, K. and Takiguchi, Y. Nucleotide sequence of the human pancreatic trypsinogen III cDNA. Nucleic Acids Res. 18 (1990) 1631. [DOI] [PMID: 2326201]
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