EC 1.1.2.8 - Alcohol dehydrogenase (cytochrome c)

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IntEnz Enzyme Nomenclature
EC 1.1.2.8

Names

Accepted name:
alcohol dehydrogenase (cytochrome c)
Other names:
type I quinoprotein alcohol dehydrogenase
quinoprotein ethanol dehydrogenase
Systematic name:
alcohol:cytochrome c oxidoreductase

Reaction

Cofactor

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 1.1.2.7, methanol dehydrogenase (cytochrome c)). It is routinely assayed with phenazine methosulphate 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 disulphide ring structure in close proximity to the PQQ.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052936 , GO:0052934 , GO:0052935
UniProtKB/Swiss-Prot:

References

  1. Rupp, M., Gorisch, H.
    Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa.
    Biol. Chem. Hoppe-Seyler 369: 431-439 (1988). [PMID: 3144289]
  2. 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: 2442-2450 (1995). [PMID: 7730276]
  3. 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: 471-481 (1999). [PMID: 10075429]
  4. Keitel, T., Diehl, A., Knaute, T., Stezowski, J. J., Hohne, W., Gorisch, H.
    X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity.
    J. Mol. Biol. 297: 961-974 (2000). [PMID: 10736230]
  5. Kay, C. W., 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: 69-72 (2004). [PMID: 15094044]
  6. Mennenga, B., Kay, C. W., 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: 361-367 (2009). [PMID: 19224199]

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