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Literature summary for 1.1.5.5 extracted from

  • Cozier, G.E.; Giles, I.G.; Anthony, C.
    The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens (1995), Biochem. J., 308, 375-379.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.5.5

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Acetobacter aceti 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a heme protein Acetobacter aceti

Organism

Organism UniProt Comment Textmining
Acetobacter aceti P18278
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in ADH, electrons pass from PQQH2 to a heme c on the same quinohemoprotein subunit, and then to ubiquinone in the membrane by way of a separate cytochrome c subunit in the three-component membrane complex, ovreview Acetobacter aceti ?
-
 ?

Synonyms

Synonyms Comment Organism
quinohaemoprotein alcohol dehydrogenase
-
 Acetobacter aceti

Cofactor

Cofactor Comment Organism Structure
heme c
-
 Acetobacter aceti
additional information an NAD(P)-independent enzyme Acetobacter aceti
pyrroloquinoline quinone PQQ, the PQQ ring is sandwiched between the indole ring of Trp245 and the two sulfur atoms of the disulfide ring structure Acetobacter aceti