KEGG   ENZYME: 3.4.22.48Help
Entry
EC 3.4.22.48                Enzyme                                 

Name
staphopain;
staphylopain
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate
Comment
Known from species of Staphylococcus. Type example of peptidase family C47.
History
EC 3.4.22.48 created 2003
Orthology
K08258  
staphopain A
Genes
SAU: 
SAV: 
SAW: 
SAH: 
SAJ: 
SAM: 
SAS: 
SAR: 
SAC: 
SACOL1970(sspB2)
SAX: 
SAA: 
SAO: 
SAE: 
NWMN_1847(sspB)
SAD: 
SAAV_1975(sspB2) SAAV_c10(scpA)
SUU: 
SUV: 
SUE: 
SUJ: 
SUK: 
SUC: 
SUT: 
SUQ: 
SUZ: 
MS7_1944(sspP)
SUD: 
SUX: 
SUW: 
SUG: 
SUF: 
SAUA: 
SAUE: 
SAUN: 
SAUS: 
SA40_1750(scpA)
SAUU: 
SAUZ: 
SAB: 
SUY: 
SAUB: 
SAUM: 
SAUC: 
SAUR: 
SEP: 
SER: 
SERP2390(sspB)
SWA: 
SPAS: 
EFD: 
RHO: 
 » show all
Taxonomy
Reference
1
  Authors
Hofmann, B., Hecht, H.J., Kiess, M. and Schomburg, D.
  Title
Crystal structure of a thiol proteinase from Staphylococcus aureus V8 in the E-64 inhibitor complex.
  Journal
Acta Crystallogr. Sect. A (Suppl.) 49 (1993) 102.
Reference
2
  Authors
Potempa, J., Dubin, A. and Travis, J.
  Title
Staphylopain.
  Journal
In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes, London, 1998, p. 669-671.
Reference
3  [PMID:11767947]
  Authors
Dubin G, Chmiel D, Mak P, Rakwalska M, Rzychon M, Dubin A.
  Title
Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis.
  Journal
Biol. Chem. 382 (2001) 1575-82.
  Organism
Staphylococcus epidermidis
  Sequence
[up:P0C0P9]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
347841-89-8

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