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Laktocepin
Identifikatori
EC broj	3.4.21.96
CAS broj	205510-58-3
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Laktocepin (EC 3.4.21.96, CEP, ektracelularna laktokokalna proteinaza, laktokokalna ćelijska wsve-asocirana proteinaza, laktokokalna proteinaza asocirana sa ćelijskim omotačem, laktokokalna proteinaza, PrtP) je enzim.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

Endopeptidazna aktivnost sa veoma širokom specifičnošću. Specifičnost se javlja u izvestnoj meri, e.g. veliki hidrofobni ostataci u P1 i P4 pozicijama, i Pro u P2 poziciji. Ovaj enzim je najbolje poznat po dejstvu na kazeine, mada je poznata da može da hidrolizuje hemoglobin i oksidovane lance insulina B

Ovaj enzim je vezan za ćelijski zid Laktococcus lactis.

Reference

↑ 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. 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. 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. PMID 8398214.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Lactocepin

[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. 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. 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. PMID 8398214.

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