Staphopain

Staphopain (EC 3.4.22.48, staphylopain) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction

Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates.
Staphopain
Identifiers
EC number3.4.22.48
CAS number347841-89-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

This enzyme is present in several species of Staphylococcus.

References

  1. Hofmann, B.; Hecht, H.J.; Kiess, M.; Schomburg, D. (1993). "Crystal structure of a thiol proteinase from Staphylococcus aureus V8 in the E-64 inhibitor complex". Acta Crystallographica Section A. 49: c102. doi:10.1107/s0108767378097081.
  2. Potempa J, Dubin A, Travis J (1998). "Staphylopain". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. pp. 669–671.
  3. Dubin G, Chmiel D, Mak P, Rakwalska M, Rzychon M, Dubin A (November 2001). "Molecular cloning and biochemical characterisation of proteases from Staphylococcus epidermidis". Biological Chemistry. 382 (11): 1575–82. doi:10.1515/bc.2001.192. PMID 11767947.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.