alcohol dehydrogenase (cytochrome c) [EC:1.1.2.8]

PMID:2001402

Tamaki T, Fukaya M, Takemura H, Tayama K, Okumura H, Kawamura Y, Nishiyama M, Horinouchi S, Beppu T

Cloning and sequencing of the gene cluster encoding two subunits of membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes.

Biochim Biophys Acta 1088:292-300 (1991)
DOI:10.1016/0167-4781(91)90066-U

PMID:7730276

Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O

Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols.

J Bacteriol 177:2442-50 (1995)
DOI:10.1128/JB.177.9.2442-2450.1995

[ag:BAF91141]

PMID:10075429

Schobert M, 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 ( Pt 2):471-81 (1999)
DOI:10.1099/13500872-145-2-471

[pae:PA1982]

Oxidoreductases;
Acting on the CH-OH group of donors;
With a cytochrome as acceptor

alcohol:cytochrome c oxidoreductase

a primary alcohol + 2 ferricytochrome c = an aldehyde + 2 ferrocytochrome c + 2 H+

(other) R05062 R05198 R05285

primary alcohol [CPD:C00226];
ferricytochrome c [CPD:C00125]

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 1.1.2.7, 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.

EC 1.1.2.8 created 1972 as 1.1.99.8, modified 1982, part transferred 2010 to EC 1.1.2.8

1  [PMID:3144289]

Rupp M, Gorisch H

Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa.

Biol. Chem. Hoppe. Seyler. 369 (1988) 431-9.

2  [PMID:7730276]

Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O

Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols.

J. Bacteriol. 177 (1995) 2442-50.

[ag:BAF91141]

3  [PMID:10075429]

Schobert M, 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 ( Pt 2) (1999) 471-81.

[pae:PA1982]

4  [PMID:10736230]

Keitel T, Diehl A, Knaute T, Stezowski JJ, Hohne W, Gorisch H

X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity.

J. Mol. Biol. 297 (2000) 961-74.

[pae:PA1982]

5  [PMID:15094044]

Kay CW, Mennenga B, Gorisch H, 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.

6  [PMID:19224199]

Mennenga B, Kay CW, 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) 361-7.