Lactocepin
Lactocepin | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.21.96 | ||||||||
CAS no. | 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 | ||||||||
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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] 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 enzyme is associated with the cell envelope of Lactococcus lactis and attached via a C-terminal membrane anchor sequence.
References
- ^ Visser S, Robben AJ, Slangen CJ (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 (4): 477–483. doi:10.1007/bf00169753. PMID 1367552.
- ^ Exterkate FA, Alting AC, Bruinenberg PG (November 1993). "Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region". Applied and Environmental Microbiology. 59 (11): 3640–7. PMC 182510. PMID 8285671.
- ^ Pritchard GG, Coolbear T (September 1993). "The physiology and biochemistry of the proteolytic system in lactic acid bacteria". FEMS Microbiology Reviews. 12 (1–3): 179–206. doi:10.1111/j.1574-6976.1993.tb00018.x. PMID 8398214.
External links
- Lactocepin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)