Lactocepin

Lactocepin
Identifiers
EC number 3.4.21.96
CAS number 205510-58-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Lactocepin (EC 3.4.21.96, CEP, extracellular lactococcal proteinase, lactococcal cell wall-associated proteinase, lactococcal cell envelope-associated proteinase, lactococcal proteinase, PrtP) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Endopeptidase activity with very broad specificity, although some subsite preferences have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position [1,2]. Best known for its action on caseins, although it has been shown to hydrolyse hemoglobin and oxidized insulin B chain

This ezyme is associated with the cell envelope of Lactococcus lactis and attached via a C-terminal membrane anchor sequence.

References

  1. Visser, S., Robben, A.J.P.M. and Slangen, C.J. (1991). "Specificity of a cell-envelope-located proteinase (PIII-type) from Lactococcus lactis' subsp. cremoris AM1 in its action on bovine β-casein". Appl. Microbiol. Biotechnol. 35: 477–483. doi:10.1007/bf00169753. PMID 1367552.
  2. Monnet, V., Ley, J.P. and Gonzalez, S. (1992). "Substrate specificity of the cell envelope-located proteinase of Lactococcus lactis' subsp. lactis NCDO763". Int. J. Biochem. 24: 707–718. doi:10.1016/0020-711x(92)90004-k. PMID 1592148.
  3. Exterkate, F.A., Alting, A.C. and Bruinenberg, P.G. (1993). "Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis' and its relationship to charge characteristics of the substrate-binding region". Appl. Environ. Microbiol. 59: 3640–3647. PMID 8285671.
  4. Pritchard, G.G. and Coolbear, T. (1993). "The physiology and biochemistry of the proteolytic system in lactic acid bacteria". FEMS Microbiol. Rev. 12: 179–206. doi:10.1111/j.1574-6976.1993.tb00018.x. PMID 8398214.

External links

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