Metanol dehidrogenaza (citohrom c)
| Metanol dehidrogenaza (citohrom c) | |||||||||
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| 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 | ||||||||
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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 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[uredi | uredi kod]
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ Cox, J.M., Day, D.J. and Anthony, C. (1992). „The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria”. Biochim. Biophys. Acta 1119: 97-106. PMID 1311606.
- ↑ 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.
- ↑ 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.
- ↑ 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 cL”. Biochemistry 40: 9799-9809. PMID 11502173.
- ↑ Anthony, C. and Williams, P. (2003). „The structure and mechanism of methanol dehydrogenase”. Biochim. Biophys. Acta 1647: 18-23. PMID 12686102.
- ↑ 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[uredi | uredi kod]
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- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
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