Dimetilanilin monooksigenaza (formiranje N-oksida)
| Dimetilanilin monooksigenaza (formiranje N-oksida) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.8 | ||||||||
| CAS broj | 37256-73-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Dimetilanilin monooksigenaza (formiranje N-oksida) (EC 1.14.13.8, dimetilanilinska oksidaza, dimetilanilinska N-oksidaza, monooksigenaza koja sadrži FAD, N,N-dimetilanilinska monooksigenaza, DMA oksidaza, flavinska oksidaza mešovite funkcije, Ziglerov enzim, aminska oksidaza mešovite funkcije, FMO, FMO-I, FMO-II, FMO1, FMO2, FMO3, FMO4, FMO5, flavinska monooksigenaza, metilfeniltetrahidropiridinska N-monooksigenaza, 1-metil-4-fenil-1,2,3,6-tetrahidropiridin:kiseonik N-oksidoreduktaza, dimetilanilinska monooksigenaza (formira N-oksid)) je enzim sa sistematskim imenom N,N-dimetilanilin,NADPH:kiseonik oksidoreduktaza (formira N-oksid).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- N,N-dimetilanilin + NADPH + H+ + O2 N,N-dimetilanilin N-oksid + NADP+ + H2O
Ovaj enzim je flavoprotein. Postoji širok spektar monooksigenaza koje mogu da deluju na znatno različite suptrate, kao što su hidrazini, fosfini, jedinjenja bora, sulfidi, selenidi, jodidi, kao i primarni, sekundarni i tercijarni amini. Ovaj enzim se razlikuje od drugih monooksigenaza po tome što formira relativno stabilne hidroperoksi flavinske intermedijere.
Reference[uredi | uredi kod]
- ↑ Ziegler, D.M. and Pettit, F.H. (1966). „Microsomal oxidases. I. The isolation and dialkylarylamine oxygenase activity of pork liver microsomes”. Biochemistry 5: 2932-2938. PMID 4381353.
- ↑ Chiba, K., Kubota, E., Miyakawa, T., Kato, Y. and Ishizaki, T. (1988). „Characterization of hepatic microsomal metabolism as an in vivo detoxication pathway of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine in mice”. J. Pharmacol. Exp. Ther. 246: 1108-1115. PMID 3262153.
- ↑ Cashman, J.R. (1995). „Structural and catalytic properties of the mammalian flavin-containing monooxygenase”. Chem. Res. Toxicol. 8: 165-181.
- ↑ Cashman, J.R. and Zhang, J. (2006). „Human flavin-containing monooxygenases”. Annu. Rev. Pharmacol. Toxicol. 46: 65-100. PMID 16402899.
- ↑ Jones, K.C. and Ballou, D.P. (1986). „Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates”. J. Biol. Chem. 261: 2553-2559. PMID 3949735.
- ↑ Chiba, K., Kobayashi, K., Itoh, K., Itoh, S., Chiba, T., Ishizaki, T. and Kamataki, T. (1995). „N-Oxygenation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine by the rat liver flavin-containing monooxygenase expressed in yeast cells”. Eur. J. Pharmacol. 293: 97-100. PMID 7672012.
Literatura[uredi | uredi kod]
- 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.