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Literature summary for extracted from

  • Kay, C.W.; Mennenga, B.; Goerisch, H.; Bittl, R.
    Substrate binding in quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa studied by electron-nuclear double resonance (2006), Proc. Natl. Acad. Sci. USA, 103, 5267-5272.
    View publication on PubMedView publication on EuropePMC


Organism UniProt Comment Textmining
Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ethanol + 2 cytochrome c EPR-study to elucidate reaction mechanism. In an addition/elimination mechanism, the negatively charged substrate oxygen then performs a nucleophilic addition to the PQQ(C5) to form a covalent substrate-PQQ complex. This is followed by elimination of ethanal, leaving the fully reduced PQQH2. In a hydride transfer mechanism, a nucleophilic addition to the PQQ(C5) again occurs, but this time it is the hydride from C1 of the substrate that is transferred, completing the oxidization of the ethanol to ethanal. Subsequently, the PQQ enolizes to form PQQH2. The results are consistent with either proposed mechanism Pseudomonas aeruginosa ethanal + 2 reduced cytochrome c