Metanol dehidrogenaza (citohrom c)

Metanol dehidrogenaza (citohrom c)
Metanol dehidrogenaza homodimer, Methylacidiphilum fumariolicum
Identifikatori
EC broj	1.1.2.7
CAS broj	37205-43-9
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

Metanol dehidrogenaza (citohrom c) (EC 1.1.2.7, MDH) je enzim sa sistematskim imenom metanol:citohrom c oksidoreduktaza.^{[1][2][3][4][5][6][7][8][9][10]} Ovaj enzim katalizuje sledeću hemijsku reakciju

primarni alkohol + 2 fericitohrom cL ${\displaystyle \rightleftharpoons }$ aldehid + 2 ferocitohrom cL + 2 H⁺

Ovaj enzim je periplazmična hinoproteinska alkoholna dehidrogenaza koja se javlja samo kod metilotrofnih bakterija. On koristi specifični citohrom cL kao acceptor i deluje na širok opseg primarnih alkohola, uključujući etanol, duodekanol, hloroetanol, cinamil alkohol, a takođe i formaldehid. Njegovu aktivnost stimuliše amonijak i metilamin. On se obično testira sa fenazin metosulfatom. Kao sve druge dehigenaze hinoproteinskog alkohola on ima strukturu propelera sa osam lopatica, jon kalcijuma vezan za PQQ u aktivnom mestu i neobičnu strukturu disulfidnog prstena u blizini PQQ. On se razlikuje od EC 1.1.2.8, alkoholne dehidrogenaze (citohroma c), po tome što ima visok afinitet za metanol, i što ima jednu dodatnu esencijalnu malu podjednicu nepoznate funkcije.

Reference

1. Anthony, C. and Zatman, L.J. (1964). „The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27”. Biochem. J. 92: 614-621. PMID 4378696. 
2. Anthony, C. and Zatman, L.J. (1967). „The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group”. Biochem. J. 104: 960-969. PMID 6049934. 
3. Duine, J.A., Frank, J. and Verweil, P.E.J. (1980). „Structure and activity of the prosthetic group of methanol dehydrogenase”. Eur. J. Biochem. 108: 187-192. PMID 6250827. 
4. Salisbury, S.A., Forrest, H.S., Cruse, W.B.T. and Kennard, O. (1979). „A novel coenzyme from bacterial primary alcohol dehydrogenases”. Nature (Lond.) 280: 843-844. PMID 471057. 
5. Cox, J.M., Day, D.J. and Anthony, C. (1992). „The interaction of methanol dehydrogenase and its electron acceptor, cytochrome c_L in methylotrophic bacteria”. Biochim. Biophys. Acta 1119: 97-106. PMID 1311606. 
6. Blake, C.C., Ghosh, M., Harlos, K., Avezoux, A. and Anthony, C. (1994). „The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues”. Nat. Struct. Biol. 1: 102-105. PMID 7656012. 
7. Xia, Z.X., He, Y.N., Dai, W.W., White, S.A., Boyd, G.D. and Mathews, F.S. (1999). „Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 Å resolution”. Biochemistry 38: 1214-1220. PMID 9930981. 
8. Afolabi, P.R., Mohammed, F., Amaratunga, K., Majekodunmi, O., Dales, S.L., Gill, R., Thompson, D., Cooper, J.B., Wood, S.P., Goodwin, P.M. and Anthony, C. (2001). „Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c_L”. Biochemistry 40: 9799-9809. PMID 11502173. 
9. Anthony, C. and Williams, P. (2003). „The structure and mechanism of methanol dehydrogenase”. Biochim. Biophys. Acta 1647: 18-23. PMID 12686102. 
10. Williams, P.A., Coates, L., Mohammed, F., Gill, R., Erskine, P.T., Coker, A., Wood, S.P., Anthony, C. and Cooper, J.B. (2005). „The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens”. Acta Crystallogr. D Biol. Crystallogr. 61: 75-79. PMID 15608378. 

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 Methanol+dehydrogenase+(cytochrome+c)