, Lys
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. Formerly EC 3.4.4.4
Links to other databases: BRENDA, EXPASY, KEGG, GTD, MEROPS, Metacyc, PDB, CAS registry number: 9002-07-7
References
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. [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 New Comprehensive Biochemistry Vol. 16, Hydrolytic Enzymes (Neuberger, A. and Brocklehurst, K. eds), pp. 159-200 (1987) Elsevier, Amsterdam
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 only. [PMID: 2326201]