Venombin A
| Venombin A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.21.74 | ||||||||
| CAS broj | 146240-35-9 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Venombin A (EC 3.4.21.74, alfa-fibrinogenaza, habutobin, cinkova metaloproteinaza Cbfib1.1, cinkova metaloproteinaza Cbfib1.2, cinkova metaloproteinaza Cbfib2, ankrod) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Selektivno razlaganje Arg- veze u fibrinogenu čime se formira fibrin, i dolazi do otpuštanja fibrinopeptida A. Specifičnost dalje degradacije fibrinogena varira u zavisnosti od porekla enzima
Ovaj enzim je donekle sličan sa trombinom. On je izolovan iz venoma zmija grupa viper/zvečarka.
Reference
- ↑ Nolan, C., Hall, L.S. and Barlow, G.H. (1976). „Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom”. Methods Enzymol. 45: 205-213. PMID 1011992.
- ↑ Stocker, K. and Barlow, G.H. (1976). „The coagulant enzyme from Bothrops atrox venom (batroxobin)”. Methods Enzymol. 45: 214-223. PMID 1011993.
- ↑ Markland, F.S., Kettner, C., Schiffmann, S., Shaw, E., Bajwa, S.S., Reddy, K.N.N., Kirakossian, H., Patkos, G.B., Theodor, I. and Pirkle, H. (1982). „Kallikrein-like activity of crotalase, a snake venom enzyme that clots fibrinogen”. Proc. Natl. Acad. Sci. USA 79: 1688-1692. PMID 7043462.
- ↑ Simmons, G., Bundalian, M., Theodor, I., Martinoli, J. and Pirkle, H. (1985). „Action of crotalase, an enzyme with thrombin-like and kallikrein-like specificities, on tripeptide nitroanilide derivatives”. Thromb. Res. 40: 555-561. PMID 2934864.
- ↑ Itoh, N., Tanaka, N., Funakoshi, I., Kawasaki, T., Mihashi, S. and Yamashina, I. (1988). „Organisation of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family”. J. Biol. Chem. 263: 7628-7631. PMID 3163691.
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 Venombin+A
- 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
