KEGG   ENZYME: 3.4.21.62Help
Entry
EC 3.4.21.62                Enzyme                                 
Name
subtilisin;
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
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides
Comment
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]
Orthology
K01342  
subtilisin
Genes
BSU: 
BSU10300(aprE)
BSR: 
BSL: 
BSS: 
BST: 
BSN: 
BSQ: 
BSUB: 
BLI: 
BL01111(apr)
BLD: 
BAO: 
BAMF_1119(aprE)
BAY: 
RBAM_010500(aprE)
BAQ: 
BACAU_1010(aprE)
BYA: 
BANAU_0954(aprE)
BAMP: 
B938_05060
BAZ: 
BAMTA208_04835(aprE)
BQL: 
LL3_01118(aprE)
BXH: 
BAXH7_01013(apr)
BQY: 
MUS_1081(aprE)
BAE: 
BATR1942_02760
BHA: 
BH0684(alp) BH0855
BCX: 
BCA_4942
BTL: 
BALH_4378
BCL: 
ABC0761(aprE)
BPU: 
BPUM_0972(aprE1)
BPF: 
BpOF4_09070(subE)
BJS: 
MY9_1131
NTH: 
Nther_2143
 » show all
Taxonomy
Reference
1
  Authors
Ottesen, M. and Svendsen, I.
  Title
The subtilisins.
  Journal
Methods Enzymol. 19 (1970) 199-215.
Reference
2
  Authors
Markland, F.S. and Smith, E.L.
  Title
Subtilisins: primary structure, chemical and physical properties.
  Journal
In: Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 3, Academic Press, New York, 1971, p. 561-608.
Reference
3  [PMID:6221910]
  Authors
Tang H.
  Title
[The use of single-dose total body irradiation before bone marrow transplantation in treatment of leukemia]
  Journal
Zhonghua. Fang. She. Xue. Za. Zhi. 16 (1982) 296-300.
Reference
4  [PMID:3927935]
  Authors
Nedkov P, Oberthur W, Braunitzer G.
  Title
Determination of the complete amino-acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN', Carlsberg and amylosacchariticus.
  Journal
Biol. Chem. Hoppe. Seyler. 366 (1985) 421-30.
  Organism
Bacillus subtilis [GN:bsu]
Reference
5  [PMID:3108260]
  Authors
Ikemura H, Takagi H, Inouye M.
  Title
Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli.
  Journal
J. Biol. Chem. 262 (1987) 7859-64.
  Organism
Bacillus subtilis [GN:bsu]
Reference
6
  Authors
Polgar, L.
  Title
Structure and function of serine proteases.
  Journal
In: Neuberger, A. and Brocklehurst, K. (Eds.), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, p. 159-200.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9014-01-1
DBGET integrated database retrieval system