Alkohol dehidrogenaza (nikotinoprotein)
(Preusmjereno sa stranice NDMA-zavisna alkoholna dehidrogenaza)
Alkohol dehidrogenaza (nikotinoprotein) (EC 1.1.99.36, NDMA-zavisna alkoholna dehidrogenaza, nikotinoprotein alkoholna dehidrogenaza, np-ADH, etanol:N,N-dimetil-4-nitrosoaniline oksidoreduktaza) je enzim sa sistematskim imenom etanol:akceptor oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Alkohol dehidrogenaza (nikotinoprotein) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.1.99.36 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- etanol + akceptor acetaldehid + redukovani akceptor
Ovaj enzim sadrži Zn2+. Dehidrogenaze nikotinoproteinskog alkohola su jedistvene dehidrogenaze/reduktaze alkohola sa lancem srednje dužine. One sadrže čvrsto vezani NAD+/NADH kofaktor koji se ne disocira tokom katalitičkog procesa. Umesto toga, kofaktor se regeneriše drugim supstratom ili nosiocem elektrona.
Reference
uredi- ↑ Van Ophem, P.W., Van Beeumen, J. and Duine, J.A. (1993). „Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica”. Eur. J. Biochem. 212: 819-826. PMID 8385013.
- ↑ Piersma, S.R., Visser, A.J., de Vries, S. and Duine, J.A. (1998). „Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase”. Biochemistry 37: 3068-3077. PMID 9485460.
- ↑ Schenkels, P. and Duine, J.A. (2000). „Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes”. Microbiology 146: 775-785. PMID 10784035.
- ↑ Piersma, S.R., Norin, A., de Vries, S., Jornvall, H. and Duine, J.A. (2003). „Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site”. J. Protein Chem. 22: 457-461. PMID 14690248.
- ↑ Norin, A., Piersma, S.R., Duine, J.A. and Jornvall, H. (2003). „Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretations”. Cell. Mol. Life Sci. 60: 999-1006. PMID 12827287.
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.