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Information on EC 3.4.21.62 - Subtilisin

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.62 Subtilisin
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UNIPROT: Q46547 not found.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyses peptide amides
Synonyms
proteinase k, subtilisin, alkaline protease, alcalase, subtilisin carlsberg, subtilase, subtilisin-like protease, savinase, alkaline serine protease, subtilisin a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
subtilisin-like protease
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Alcalase
-
-
-
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Alcalase 0.6L
-
-
-
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Alcalase 2.5L
-
-
-
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ALK-enzyme
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-
-
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Alkaline mesentericopeptidase
-
-
-
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Alkaline protease
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-
-
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Bacillopeptidase A
-
-
-
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Bacillopeptidase B
-
-
-
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Bacillus subtilis alkaline proteinase Bioprase
-
-
-
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Bioprase AL 15
-
-
-
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Bioprase APL 30
-
-
-
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Colistinase
-
-
-
-
Esperase
-
-
-
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Genenase I
-
-
-
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Kazusase
-
-
-
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Maxatase
-
-
-
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Nagarse
-
-
-
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Opticlean
-
-
-
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Orientase 10B
-
-
-
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Peptidase, subtilo-, A
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-
-
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Protease S
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-
-
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Protease VIII
-
-
-
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Protease XXVII
-
-
-
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Proteinase, Bacillus subtilis alkaline
-
-
-
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Protin A 3L
-
-
-
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Savinase
-
-
-
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Savinase 16.0L
-
-
-
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Savinase 32.0 L EX
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-
-
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Savinase 4.0T
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-
-
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Savinase 8.0L
-
-
-
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SP 266
-
-
-
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Subtilisin E
-
-
-
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Subtilisin GX
-
-
-
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Subtilisin Novo
-
-
-
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Subtilisin S41
-
-
-
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Subtilisin Sendai
-
-
-
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Subtilopeptidase
-
-
-
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Superase
-
-
-
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Thermoase
-
-
-
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Thermoase PC 10
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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ester bond hydrolysis
-
-
-
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transpeptidation
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-
-
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transesterification
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9014-01-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + p-nitroaniline
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
required for catalysis
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
BprB
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
strains causing benign footrot secrete subtilisin-like protease BprB
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q46547_DICNO
603
0
63608
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by the hanging-drop vapour-diffusion method. Crystals of BprB diffract to 1.8 A resolution. The crystals belong to space group P21, with unit-cell parameters a = 38.5, b = 90.5, c = 44.1 A , beta = 109.9. The crystals contain one molecule in the asymmetric unit, with a solvent content of 36%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
vector pET22b-BprB encoded residues 1-476 of BprB with a C-terminal His6 tag transformed into Escherichia coli strain Rosetta-Gami(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wong, W.; Kennan, R.M.; Rosado, C.J.; Rood, J.I.; Whisstock, J.C.; Porter, C.J.
Crystallization of the virulent and benign subtilisin-like proteases from the ovine footrot pathogen Dichelobacter nodosus
Acta Crystallogr. Sect. F
66
289-293
2010
Dichelobacter nodosus, Dichelobacter nodosus (A5EVD0), Dichelobacter nodosus (A5EXI3), Dichelobacter nodosus (Q46547), Dichelobacter nodosus C305 (Q46547), Dichelobacter nodosus VCS1703A (A5EVD0), Dichelobacter nodosus VCS1703A (A5EXI3)
Manually annotated by BRENDA team