メタノールデヒドロゲナーゼ (シトクロムc)
| メタノールデヒドロゲナーゼ (シトクロムc) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 識別子 | |||||||||
| EC番号 | 1.1.2.7 | ||||||||
| データベース | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB構造 | RCSB PDB PDBj PDBe PDBsum | ||||||||
| |||||||||
メタノールデヒドロゲナーゼ (シトクロムc)(methanol dehydrogenase (cytochrome c))は、次の化学反応を触媒する酵素である。
- 第一級アルコール + 2 シトクロムcL アルデヒド + 2 還元型シトクロムcL
この酵素の基質は第一級アルコールとシトクロムcLで、生成物はアルデヒドと還元型シトクロムcLである。
この酵素は酸化還元酵素に属し、シトクロムを受容体として供与体であるCH-OH基に特異的に作用する。組織名はmethanol:cytochrome c oxidoreductaseで、別名にmethanol dehydrogenase、MDHがある。
参考文献[編集]
- 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 c(L).”. 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.