Lactocepin
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
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
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