Subtilisin Savinase

Details

Name
Subtilisin Savinase
Synonyms
  • 3.4.21.62
  • Alkaline protease
Gene Name
Not Available
Organism
Bacillus lentus
Amino acid sequence
>lcl|BSEQ0010890|Subtilisin Savinase
AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN
GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVA
NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGAGSISYPARYANAMAVGATDQNNNR
ASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI
RNHLKNTATSLGSTNLYGSGLVNAEAATR
Number of residues
269
Molecular Weight
26698.32
Theoretical pI
9.63
GO Classification
Functions
metal ion binding / serine-type endopeptidase activity
Processes
sporulation resulting in formation of a cellular spore
Components
extracellular region
General Function
Serine-type endopeptidase activity
Specific Function
Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP29600
UniProtKB Entry NameSUBS_BACLE
General References
  1. Betzel C, Klupsch S, Papendorf G, Hastrup S, Branner S, Wilson KS: Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4 A resolution. J Mol Biol. 1992 Jan 20;223(2):427-45. [Article]
  2. Remerowski ML, Pepermans HA, Hilbers CW, Van De Ven FJ: Backbone dynamics of the 269-residue protease Savinase determined from 15N-NMR relaxation measurements. Eur J Biochem. 1996 Feb 1;235(3):629-40. [Article]
  3. Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R: The 0.78 A structure of a serine protease: Bacillus lentus subtilisin. Biochemistry. 1998 Sep 29;37(39):13446-52. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01973O-Benzylsulfonyl-SerineexperimentalunknownDetails