The Enzyme Database

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EC 3.4.22.10     
Accepted name: streptopain
Reaction: Preferential cleavage with hydrophobic residues at P2, P1 and P1′
Other name(s): Streptococcus peptidase A; streptococcal cysteine proteinase; Streptococcus protease
Comments: From the bacterium, group A Streptococcus. Formed from the proenzyme by limited proteolysis. Type example of peptidase family C10.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-51-8
References:
1.  Elliott, S.D. and Liu, T.-Y. Streptococcal proteinase. Methods Enzymol. 19 (1970) 252–261.
2.  Liu, T.-Y. and Elliott, S.D. Streptococcal proteinase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, Academic Press, New York, 1971, pp. 609–647.
3.  Tai, J. Y., Kortt, A.A., Liu, T.-Y. and Elliott, S.D. Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain. J. Biol. Chem. 251 (1976) 1955–1959. [PMID: 1270417]
4.  Lo, S.-S., Fraser, B.A. and Liu, T.-Y. The mixed disulphide in the zymogen of streptococcal proteinase. Characterization and implication for its biosynthesis. J. Biol. Chem. 259 (1984) 11041–11045. [PMID: 6381494]
[EC 3.4.22.10 created 1961 as EC 3.4.4.18, transferred 1972 to EC 3.4.22.10]
 
 


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