EC 3.4.21.4 - Trypsin
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.4.21.4
Names
Accepted name:
trypsin
Other
names:
α-trypsin
β-trypsin
cocoonase
parenzyme
parenzymol
pseudotrypsin
sperm receptor hydrolase
tripcellim
tryptar
tryptase
trypure
β-trypsin
cocoonase
parenzyme
parenzymol
pseudotrypsin
sperm receptor hydrolase
tripcellim
tryptar
tryptase
trypure
Systematic name:
-
Reaction
- Preferential cleavage: Arg, Lys.
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
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
MEROPS
,
NIST 74
,
UniPathway
Protein domains and families:
PROSITE:PDOC00124
Gene Ontology:
GO:0004252
CAS Registry Number:
9002-07-7
References
-
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 Biochemistry vol. 16 , Elsevier , Amsterdam , 1987 , 159-200 -
Nucleotide sequence of the human pancreatic trypsinogen III cDNA.Nucleic Acids Res. 18 : 1631 (1990). [PMID: 2326201]
[EC 3.4.21.4 created 1961 as EC 3.4.4.4, transferred 1972 to EC 3.4.21.4]