Subtilisin

Peptidase S8, subtilisin-related
S8 + I9 (lower-right), Bacillus subtilis (PDB: 2pmw​)
Identifiers
SymbolPeptidase_S8
PfamPF00082
InterProIPR015500
PROSITEPDOC00125
CATH1cse
SCOP21cse / SCOPe / SUPFAM
CDDcd07477
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Subtilisin BPN'
Crystal structure of subtilisin S8 domain.[1]
Identifiers
OrganismBacillus amyloliquefaciens
Symbolapr
CAS number9014-01-1
Entrez5712479
PDB1st2 More structures
UniProtP00782
Other data
EC number3.4.21.62
Search for
StructuresSwiss-model
DomainsInterPro
GO:0004252

Subtilisin is a protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis.[2][3][4][5][6][7][8]

Subtilisins belong to subtilases, a group of serine proteases that – like all serine proteases – initiate the nucleophilic attack on the peptide (amide) bond through a serine residue at the active site. Subtilisins typically have molecular weights 27kDa. They can be obtained from certain types of soil bacteria, for example, Bacillus amyloliquefaciens from which they are secreted in large amounts.

  1. ^ PDB: 1st2​; Bott R, Ultsch M, Kossiakoff A, Graycar T, Katz B, Power S (June 1988). "The three-dimensional structure of Bacillus amyloliquefaciens subtilisin at 1.8 A and an analysis of the structural consequences of peroxide inactivation". The Journal of Biological Chemistry. 263 (16): 7895–906. doi:10.1016/S0021-9258(18)68582-5. PMID 3286644.
  2. ^ Ottesen M, Svendsen I (1970). The subtilisins. Methods Enzymol. Vol. 19. pp. 199–215. doi:10.1016/0076-6879(70)19014-8. ISBN 978-0-12-181881-4.
  3. ^ Markland FS, Smith EL (1971). "Subtilisins: primary structure, chemical and physical properties". In Boyer PD (ed.). The Enzymes. Vol. 3 (3rd ed.). New York: Academic Press. pp. 561–608.
  4. ^ Philipp M, Bender ML (1983). "Kinetics of subtilisin and thiolsubtilisin". Molecular and Cellular Biochemistry. 51 (1): 5–32. doi:10.1007/bf00215583. PMID 6343835. S2CID 24136200.
  5. ^ Nedkov P, Oberthür W, Braunitzer G (April 1985). "Determination of the complete amino-acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN', Carlsberg and amylosacchariticus". Biological Chemistry Hoppe-Seyler. 366 (4): 421–30. doi:10.1515/bchm3.1985.366.1.421. PMID 3927935.
  6. ^ Ikemura H, Takagi H, Inouye M (June 1987). "Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli". The Journal of Biological Chemistry. 262 (16): 7859–64. doi:10.1016/S0021-9258(18)47646-6. PMID 3108260.
  7. ^ Polgár L (1987). "Structure and function of serine proteases". In Brocklehurst K, Neuberger A (eds.). Hydrolytic enzymes. Amsterdam: Elsevier. ISBN 0-444-80886-8.
  8. ^ Vasantha N, Thompson LD, Rhodes C, Banner C, Nagle J, Filpula D (September 1984). "Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein". Journal of Bacteriology. 159 (3): 811–9. doi:10.1128/JB.159.3.811-819.1984. PMC 215730. PMID 6090391.