Koenzim-B sulfoetiltiotransferaza
| Koenzim-B sulfoetiltiotransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.8.4.1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Koenzim-B sulfoetiltiotransferaza (EC 2.8.4.1, metil-KoM reduktaza, metil koenzim M reduktaza) je enzim sa sistematskim imenom metil-KoM:CoB S-(2-sulfoetil)tiotransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- metil-KoM + CoB KoM-S-S-CoB + metan
Ovaj enzim katalizuje finalni korak metanogeneze.
Reference
- ↑ Bobik, T.A., Olson, K.D., Noll, K.M. and Wolfe, R.S. (1987). „Evidence that the heterodisulfide of coenzyme-M and 7-mercaptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium”. Biochem. Biophys. Res. Commun. 149: 455-460. PMID 3122735.
- ↑ Ellermann, J., Hedderich, R., Boecher, R. and Thauer, R.K. (1988). „The final step in methane formation: investigations with highly purified methyl coenzyme M reductase component C from Methanobacterium thermoautotrophicum (strain Marburg)”. Eur. J. Biochem. 184: 63-68.
- ↑ Ermler, U., Grabarse, W., Shima, S., Goubeaud, M. and Thauer, R.K. (1997). „Crystal structure of methyl coenzyme M reductase: The key enzyme of biological methane formation”. Science 278: 1457-1462. PMID 9367957.
- ↑ Signor, L., Knuppe, C., Hug, R., Schweizer, B., Pfaltz, A. and Jaun, B. (2000). „Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate — a process mimicking methanogenesis in Archaea”. Chemistry 6: 3508-3516. PMID 11072815.
- ↑ Scheller, S., Goenrich, M., Boecher, R., Thauer, R.K. and Jaun, B. (2010). „The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane”. Nature 465: 606-608. PMID 20520712.
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 Coenzyme-B+sulfoethylthiotransferase
- 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
