(Metil-Co(III) metilamin-specifični korinoid protein):koenzim M metiltransferaza
Изглед
(Metil-Co(III) metilamin-specifični korinoid protein):koenzim M metiltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.1.1.247 | ||||||||
Baze podataka | |||||||||
IntEnz | IntEnz pregled | ||||||||
BRENDA | BRENDA pristup | ||||||||
ExPASy | NiceZyme pregled | ||||||||
KEGG | KEGG pristup | ||||||||
MetaCyc | metabolički put | ||||||||
PRIAM | profil | ||||||||
Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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(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 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
[уреди | уреди извор]- ^ Burke, S.A. & 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. & 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. & 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
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
[уреди | уреди извор]- (methyl-Co(III)+methylamine-specific+corrinoid+protein):coenzyme+M+methyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)