Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 | |
antimycin A | inhibits Q2H2 oxidation and Q reduction | Gluconobacter oxydans | |
Triton X-100 | - |
Gluconobacter oxydans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | quinone reduction kinetics, overview | Gluconobacter oxydans | |
0.0035 | - |
pyrroloquinoline quinone | pH 5.0, 25°C, quinone-bound enzyme, in presence of N-dodecyl-beta-D-maltoside | Gluconobacter oxydans | |
0.0035 | - |
pyrroloquinoline quinone | ubiquinone-bound enzyme, in the presence of dodecylmaltoside, at pH 5.0 and 25°C | Gluconobacter oxydans | |
0.0064 | - |
pyrroloquinoline quinone | pH 5.0, 25°C, quinone-free enzyme, in presence of N-dodecyl-beta-D-maltoside | Gluconobacter oxydans | |
0.0064 | - |
pyrroloquinoline quinone | Ubiquinone-free enzyme, in the presence of dodecylmaltoside, at pH 5.0 and 25°C | Gluconobacter oxydans | |
0.0117 | - |
pyrroloquinoline quinone | pH 5.0, 25°C, quinone-free enzyme, in presence of Triton X-100 | Gluconobacter oxydans | |
0.0117 | - |
pyrroloquinoline quinone | Triton X-100-purified enzyme, without bound ubiquinone, at pH 5.0 and 25°C | Gluconobacter oxydans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | bound | Gluconobacter oxydans | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + ubiquinone | Gluconobacter oxydans | the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity | acetaldehyde + ubiquinol | - |
? | |
ethanol + ubiquinone | Gluconobacter oxydans IFO 12528 | the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity | acetaldehyde + ubiquinol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gluconobacter oxydans | - |
constitutive enzyme | - |
Gluconobacter oxydans IFO 12528 | - |
constitutive enzyme | - |
Purification (Comment) | Organism |
---|---|
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + pyrroloquinoline quinone | - |
Gluconobacter oxydans | acetaldehyde + pyrroloquinoline quinol | - |
r | |
ethanol + pyrroloquinoline quinone | - |
Gluconobacter oxydans IFO 12528 | acetaldehyde + pyrroloquinoline quinol | - |
r | |
ethanol + ubiquinone | the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity | Gluconobacter oxydans | acetaldehyde + ubiquinol | - |
? | |
ethanol + ubiquinone | electron transfer mechanism, intramolecular transfer of electrons from pyrroloquinoline quinone to ubiquinone and the quinone binding sites, overview | Gluconobacter oxydans | acetaldehyde + ubiquinol | - |
? | |
ethanol + ubiquinone | the enzyme is required for the non-energy producing, cyanide-insensitive bypass oxidase activity | Gluconobacter oxydans IFO 12528 | acetaldehyde + ubiquinol | - |
? | |
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 | Comment | Organism |
---|---|---|
Q-bound ADH | - |
- |
quinoprotein alcohol dehydrogenase | - |
Gluconobacter oxydans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Gluconobacter oxydans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
assay at | Gluconobacter oxydans |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3.5 | 7 | - |
Gluconobacter oxydans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme c | four heme c per enzyme involved in electron transfer for ubiquinone reduction and ubiquinol oxidation | Gluconobacter oxydans | |
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 | |
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] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibition kinetics | Gluconobacter oxydans |