ExplorEnz: EC 3.4.22.10

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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, Gene, 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]