Formilmetanofuran dehidrogenaza
| Formilmetanofuran dehidrogenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.2.99.5 | ||||||||
| CAS broj | 119940-12-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Formilmetanofuran dehidrogenaza (EC 1.2.99.5, formilmethanofuran:(akceptor) oksidoreduktaza) je enzim sa sistematskim imenom formilmethanofuran:akceptor oksidoreduktaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- formilmetanofuran + H2O + akceptor CO2 + metanofuran + redukovani akceptor
Ovaj molibdoprotein sadrži pterinski kofactor. Volfram može da zameni molibden. Ovaj enzim katalizuje reverzibilnu reakciju u metanogenim bakterijama, i učestvuje u metanogenezi iz CO2 kao i oksidaciji metil-koenzima M do CO2. Metil viologen može da deluje kao akceptor. Ovaj enzim takođe oksiduje N-furfurilformamid.
Reference
- ↑ Karrasch, M., Börner, G., Enssle, M. and Thauer, R.K. (1990). „The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor”. Eur. J. Biochem. 194: 367-372. PMID 2125267.
- ↑ Bertram, P.A., Schmitz, R.A., Linder, D. and Thauer, R.K. (1994). „Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase”. Arch. Microbiol. 161: 220-228. PMID 8161283.
- ↑ Bertram, P.A., Karrasch, M., Schmitz, R.A., Bocher, R., Albracht, S.P. and Thauer, R.K. (1994). „Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins”. Eur. J. Biochem. 220: 477-484. PMID 8125106.
- ↑ Vorholt, J.A. and Thauer, R.K. (1997). „The active species of ’CO2’ utilized by formylmethanofuran dehydrogenase from methanogenic Archaea”. Eur. J. Biochem. 248: 919-924. PMID 9342247.
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 Formylmethanofuran+dehydrogenase
- 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
