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Literature summary extracted from

  • Matsushita, K.; Kobayashi, Y.; Mizuguchi, M.; Toyama, H.; Adachi, O.; Sakamoto, K.; Miyoshi, H.
    A tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans (2008), Biosci. Biotechnol. Biochem., 72, 2723-2731.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.5.5 2,6-dichloro-4-dicyanovinylphenol i.e. PC-16, competitive quinone reduction inhibition mode, the inhibitor binds to the low affinity quinone binding site(S) QN and/or QL of quinone-bound ADH, overview Gluconobacter oxydans
1.1.5.5 antimycin A inhibits Q2H2 oxidation and Q reduction Gluconobacter oxydans
1.1.5.5 Triton X-100
-
Gluconobacter oxydans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.5 additional information
-
additional information quinone reduction kinetics, overview Gluconobacter oxydans
1.1.5.5 0.0035
-
pyrroloquinoline quinone pH 5.0, 25°C, quinone-bound enzyme, in presence of N-dodecyl-beta-D-maltoside Gluconobacter oxydans
1.1.5.5 0.0035
-
pyrroloquinoline quinone ubiquinone-bound enzyme, in the presence of dodecylmaltoside, at pH 5.0 and 25°C Gluconobacter oxydans
1.1.5.5 0.0064
-
pyrroloquinoline quinone pH 5.0, 25°C, quinone-free enzyme, in presence of N-dodecyl-beta-D-maltoside Gluconobacter oxydans
1.1.5.5 0.0064
-
pyrroloquinoline quinone Ubiquinone-free enzyme, in the presence of dodecylmaltoside, at pH 5.0 and 25°C Gluconobacter oxydans
1.1.5.5 0.0117
-
pyrroloquinoline quinone pH 5.0, 25°C, quinone-free enzyme, in presence of Triton X-100 Gluconobacter oxydans
1.1.5.5 0.0117
-
pyrroloquinoline quinone Triton X-100-purified enzyme, without bound ubiquinone, at pH 5.0 and 25°C Gluconobacter oxydans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.5 membrane bound Gluconobacter oxydans 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.5 ethanol + ubiquinone Gluconobacter oxydans the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone Gluconobacter oxydans IFO 12528 the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity acetaldehyde + ubiquinol
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.5 Gluconobacter oxydans
-
constitutive enzyme
-
1.1.5.5 Gluconobacter oxydans IFO 12528
-
constitutive enzyme
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.5 quinone-bound and quinone-free native enzyme from membranes, purification of an active enzyme is successful with N-dodecyl beta-D-maltoside, but not with Triton X-100 Gluconobacter oxydans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.5 ethanol + pyrroloquinoline quinone
-
Gluconobacter oxydans acetaldehyde + pyrroloquinoline quinol
-
r
1.1.5.5 ethanol + pyrroloquinoline quinone
-
Gluconobacter oxydans IFO 12528 acetaldehyde + pyrroloquinoline quinol
-
r
1.1.5.5 ethanol + ubiquinone the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity Gluconobacter oxydans acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone electron transfer mechanism, intramolecular transfer of electrons from pyrroloquinoline quinone to ubiquinone and the quinone binding sites, overview Gluconobacter oxydans acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity Gluconobacter oxydans IFO 12528 acetaldehyde + ubiquinol
-
?
1.1.5.5 ethanol + ubiquinone electron transfer mechanism, intramolecular transfer of electrons from pyrroloquinoline quinone to ubiquinone and the quinone binding sites, overview Gluconobacter oxydans IFO 12528 acetaldehyde + ubiquinol
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.5 Q-bound ADH
-
-
1.1.5.5 quinoprotein alcohol dehydrogenase
-
Gluconobacter oxydans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.5.5 25
-
assay at Gluconobacter oxydans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.5 5
-
assay at Gluconobacter oxydans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.5.5 3.5 7
-
Gluconobacter oxydans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.5 heme c four heme c per enzyme involved in electron transfer for ubiquinone reduction and ubiquinol oxidation Gluconobacter oxydans
1.1.5.5 pyrroloquinoline quinone PQQ, active in electron transfer, a tightly bound ubiquinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase. The enzyme possesses distinct quinone oxidation, reduction and high affinity binding sites, analysis, overview Gluconobacter oxydans
1.1.5.5 ubiquinone the enzyme has a high affinity ubiquinone binding site besides low-affinity ubiquinone reduction and ubiquinol oxidation sites. The bound ubiquinone in the ubiquinol site is involved in the electron transfer between heme c moieties and bulk ubiquinone or ubiquinol in the low affinity sites Gluconobacter oxydans

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.5.5 additional information
-
additional information inhibition kinetics Gluconobacter oxydans