(Metil-Co(III) metilamin-specifični korinoid protein):koenzim M metiltransferaza
(Preusmjereno sa stranice MT2-A)
(Metil-Co(III) metilamin-specifični korinoid protein):koenzim M metiltransferaza (EC 2.1.1.247, metiltransferaza 2, MT2, MT2-A, mtbA (gen)) je enzim sa sistematskim imenom korinoidni protein specifičan za metilisani monometilamin:koenzim M metiltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
| (Metil-Co(III) metilamin-specifični korinoid protein):koenzim M metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.247 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- [metil-Co(III) metilamin-specifični korinoidni protein] + koenzim M metil-KoM + [Co(I) metilamin-specifični korinoidni protein]
Ovaj enzim sadrži cink. Enzim koji učestvuje u metanogenezi sa mono-, di-, i trimetilamina, katalizuje transfer metil grupa vezanih za kobaltni kofaktor nekoliko korinoidnih proteina.
Reference
uredi- ↑ Burke, S.A. and Krzycki, J.A. (1995). „Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine”. J. Bacteriol. 177: 4410-4416. PMID 7635826.
- ↑ LeClerc, G.M. and Grahame, D.A. (1996). „Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression”. J. Biol. Chem. 271: 18725-18731. PMID 8702528.
- ↑ Ferguson, D.J., Jr. and Krzycki, J.A. (1997). „Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri”. J. Bacteriol. 179: 846-852. PMID 9006042.
- ↑ Burke, S.A., Lo, S.L. and Krzycki, J.A. (1998). „Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine”. J. Bacteriol. 180: 3432-3440. PMID 9642198.
- ↑ Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. (2000). „Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri”. J. Biol. Chem. 275: 29053-29060. PMID 10852929.
Literatura
uredi- 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.