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
Pretraga PMC articles PubMed articles NCBI Protein search

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 ${\displaystyle \rightleftharpoons }$ 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

1. 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. 
2. 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. 
3. Cashman, J.R. (1995). „Structural and catalytic properties of the mammalian flavin-containing monooxygenase”. Chem. Res. Toxicol. 8: 165-181. 
4. Cashman, J.R. and Zhang, J. (2006). „Human flavin-containing monooxygenases”. Annu. Rev. Pharmacol. Toxicol. 46: 65-100. PMID 16402899. 
5. 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. 
6. 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

• 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 Flavin-containing+monooxygenase