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Trimetilamin monooksigenaza
Identifikatori
EC broj	1.14.13.148
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Trimetilamin monooksigenaza (EC 1.14.13.148, flavinska monooksigenaza 3, FMO3, tmm (gen)) je enzim sa sistematskim imenom N,N,N-trimetilamin,NADPH:kiseonik oksidoreduktaza (formira N-oksid).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

N,N,N-trimetilamin + NADPH + H⁺ + O₂

\rightleftharpoons

N,N,N-trimetilamin N-oksid + NADP⁺ + H₂O

Ovaj enzim je flavoprotein. Bakterijski enzim omogućava bakterijama da koriste trimetilamin kao jedini izvor ugljenika i energije.

Reference

↑ Large, P.J., Boulton, C.A. and Crabbe, M.J. (1972). „The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans”. Biochem. J. 128: 137P-138P. PMID 4404764.
↑ Dolphin, C.T., Riley, J.H., Smith, R.L., Shephard, E.A. and Phillips, I.R. (1997). „Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA”. Genomics 46: 260-267. PMID 9417913.
↑ Treacy, E.P., Akerman, B.R., Chow, L.M., Youil, R., Bibeau, C., Lin, J., Bruce, A.G., Knight, M., Danks, D.M., Cashman, J.R. and Forrest, S.M. (1998). „Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication”. Hum. Mol. Genet. 7: 839-845. PMID 9536088.
↑ Chen, Y., Patel, N.A., Crombie, A., Scrivens, J.H. and Murrell, J.C. (2011). „Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase”. Proc. Natl. Acad. Sci. USA 108: 17791-17796. PMID 22006322.

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.

Vanjske veze

MeSH Trimethylamine+monooxygenase

[1] Large, P.J., Boulton, C.A. and Crabbe, M.J. (1972). „The reduced nicotinamide-adenine dinucleotide phosphate- and oxygen-dependent N-oxygenation of trimethylamine by Pseudomonas aminovorans”. Biochem. J. 128: 137P-138P. PMID 4404764.

[2] Dolphin, C.T., Riley, J.H., Smith, R.L., Shephard, E.A. and Phillips, I.R. (1997). „Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA”. Genomics 46: 260-267. PMID 9417913.

[3] Treacy, E.P., Akerman, B.R., Chow, L.M., Youil, R., Bibeau, C., Lin, J., Bruce, A.G., Knight, M., Danks, D.M., Cashman, J.R. and Forrest, S.M. (1998). „Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication”. Hum. Mol. Genet. 7: 839-845. PMID 9536088.

[4] Chen, Y., Patel, N.A., Crombie, A., Scrivens, J.H. and Murrell, J.C. (2011). „Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase”. Proc. Natl. Acad. Sci. USA 108: 17791-17796. PMID 22006322.

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