Laktocepin
| 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 | ||||||||
| |||||||||
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.
Spoljašnje veze
- MeSH Lactocepin
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
