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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: Q9S3L6 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
Alcalase
-
-
-
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Alcalase 0.6L
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-
-
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Alcalase 2.5L
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-
-
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ALK-enzyme
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-
-
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Alkaline mesentericopeptidase
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-
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Alkaline protease
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-
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Bacillopeptidase A
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-
-
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Bacillopeptidase B
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-
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Bacillus subtilis alkaline proteinase Bioprase
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-
-
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Bioprase AL 15
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Bioprase APL 30
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-
-
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Colistinase
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-
-
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Esperase
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-
-
-
Genenase I
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-
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Kazusase
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-
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Maxatase
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-
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Nagarse
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-
-
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Opticlean
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-
-
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Orientase 10B
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-
-
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Peptidase, subtilo-, A
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Protease S
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Protease VIII
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-
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Protease XXVII
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-
-
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Proteinase, Bacillus subtilis alkaline
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-
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Protin A 3L
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-
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Savinase
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-
-
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Savinase 16.0L
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-
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Savinase 32.0 L EX
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Savinase 4.0T
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-
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Savinase 8.0L
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-
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SP 266
-
-
-
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Subtilisin E
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-
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Subtilisin GX
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-
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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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-
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Thermoase
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Thermoase PC 10
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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ester bond hydrolysis
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transpeptidation
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transesterification
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CAS REGISTRY NUMBER
COMMENTARY hide
9014-01-1
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
calcium-loaded state of five ions bound to each of the two subtilisin molecules. Three of the binding sites have two side chains of an acidic residue coordinating the calcium ion, whereas the other two binding sites have either a main-chain carbonyl, or only one acidic residue side chain coordinating the calcium ion
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9S3L6_LYSSH
431
0
45345
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by the hanging drop vapor-diffusion method, at 0.8 A resolution. Crystals belong to the monoclinic space group P21. Unit cell parameters are a = 46.09 A, b = 62.67 A, c = 84.87 A, and beta = 95.5°, indicating two molecules of Sph in the asymmetric unit. The crystal structures of the psychrophilic Bacillus TA41 subtilisin S41 and the mesophilic subtilisin Sph are nearly identical with the same calcium-loaded state in that five calcium ions are bound to each protein molecule
by the hanging drop vapor-diffusion method, at 1.4 A resolution. Crystals belong to either the tetragonal space group P41212 or P43212. Unit cell dimensions are a = b = 61 A and c = 174.77 A , indicating one monomer in the asymmetric unit. The crystal structures of the psychrophilic subtilisin S41 and the mesophilic Bacillus sphaericus subtilisin Sph are nearly identical with the same calcium-loaded state in that five calcium ions are bound to each protein molecule
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Almog, O.; Gonzalez, A.; Godin, N.; De Leeuw, M.; Mekel, M.; Klein, D.; Braun, S.; Shoham, G.; Walter, R.
The crystal structures of the psychrophilic subtilisin S41 and the mesophilic subtilisin Sph reveal the same calcium-loaded state
Proteins
74
489-496
2009
Lysinibacillus sphaericus (Q9S3L6), Lysinibacillus sphaericus
Manually annotated by BRENDA team