The Enzyme Database

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Accepted name: alcohol dehydrogenase (cytochrome c)
Reaction: a primary alcohol + 2 ferricytochrome c = an aldehyde + 2 ferrocytochrome c + 2 H+
Other name(s): type I quinoprotein alcohol dehydrogenase; quinoprotein ethanol dehydrogenase
Systematic name: alcohol:cytochrome c oxidoreductase
Comments: A periplasmic PQQ-containing quinoprotein. Occurs in Pseudomonas and Rhodopseudomonas. The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c550 as electron acceptor. Acts on a wide range of primary and secondary alcohols, but not methanol. It has a homodimeric structure [contrasting with the heterotetrameric structure of EC, methanol dehydrogenase (cytochrome c)]. It is routinely assayed with phenazine methosulfate as electron acceptor. Activity is stimulated by ammonia or amines. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed ’propeller’ structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
1.  Rupp, M. and Gorisch, H. Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa. Biol. Chem. Hoppe-Seyler 369 (1988) 431–439. [PMID: 3144289]
2.  Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols. J. Bacteriol. 177 (1995) 2442–2450. [DOI] [PMID: 7730276]
3.  Schobert, M. and Gorisch, H. Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase. Microbiology 145 (1999) 471–481. [DOI] [PMID: 10075429]
4.  Keitel, T., Diehl, A., Knaute, T., Stezowski, J.J., Hohne, W. and Gorisch, H. X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity. J. Mol. Biol. 297 (2000) 961–974. [DOI] [PMID: 10736230]
5.  Kay, C.W., Mennenga, B., Gorisch, H. and Bittl, R. Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy. FEBS Lett. 564 (2004) 69–72. [DOI] [PMID: 15094044]
6.  Mennenga, B., Kay, C.W. and Gorisch, H. Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550. Arch. Microbiol. 191 (2009) 361–367. [DOI] [PMID: 19224199]
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