The Enzyme Database

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EC 3.4.21.62     
Accepted name: subtilisin
Reaction: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides
Other name(s): alcalase; alcalase 0.6L; alcalase 2.5L; ALK-enzyme; bacillopeptidase A; bacillopeptidase B; Bacillus subtilis alkaline proteinase bioprase; bioprase AL 15; bioprase APL 30; colistinase; (see also comments); subtilisin J; subtilisin S41; subtilisin Sendai; subtilisin GX; subtilisin E; subtilisin BL; genenase I; esperase; maxatase; alcalase; thermoase PC 10; protease XXVII; thermoase; superase; subtilisin DY; subtilopeptidase; SP 266; savinase 8.0L; savinase 4.0T; kazusase; protease VIII; opticlean; Bacillus subtilis alkaline proteinase; protin A 3L; savinase; savinase 16.0L; savinase 32.0 L EX; orientase 10B; protease S
Comments: Subtilisin is a serine endopeptidase, type example of peptidase family S8. It contains no cysteine residues (although these are found in homologous enzymes). Species variants include subtilisin BPN′ (also subtilisin B, subtilopeptidase B, subtilopeptidase C, Nagarse, Nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species [1,3]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9014-01-1
References:
1.  Ottesen, M. and Svendsen, I. The subtilisins. Methods Enzymol. 19 (1970) 199–215.
2.  Markland, F.S. and Smith, E.L. Subtilisins: primary structure, chemical and physical properties. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 3, Academic Press, New York, 1971, pp. 561–608.
3.  Philipp, M. and Bender, M.L. Kinetics of subtilisin and thiolsubtilisin. Mol. Cell. Biochem. 51 (1983) 5–32. [PMID: 6221910]
4.  Nedkov, P., Oberthür, W. and Braunitzer, G. Determination of the complete amino acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN, Carlsberg and amylosacchariticus. Biol. Chem. Hoppe-Seyler 366 (1985) 421–430. [PMID: 3927935]
5.  Ikemura, H., Takagi, H. and Inouye, M. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. J. Biol. Chem. 262 (1987) 7859–7864. [PMID: 3108260]
6.  Polgár, L. Structure and function of serine proteases. In: Neuberger, A. and Brocklehurst, K. (Eds), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, pp. 159–200.
[EC 3.4.21.62 created 1992 (EC 3.4.21.14 created 1961 as EC 3.4.4.16, transferred 1972 to EC 3.4.21.14, modified 1986, part incorporated 1992)]
 
 


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