Cloned (Comment) | Organism |
---|---|
gene quiA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, heterologous expression of QDH in Gluconobacter frateurii, improvement of the heterologous expression of QDH in Gluconobacter strains using a broad-host-range plasmid, best with a long 5'-UTR. Gluconobacter oxydans strain NBRC12528 DELTAadhA::KmR is transformed by triparental mating using Escherichia coli HB101 harboring pRK2013 as the helper strain, Gluconobacter frateurii strain SEI46 (DELTAadhAB) is transformed with the same plasmids by electroporation | Gluconobacter oxydans |
gene quiA, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, QDH translates from the second TTG codon: Met-His-Ser-Ile-Asp, heterologous expression of QDH in Gluconobacter frateurii, improvement of the heterologous expression of QDH in Gluconobacter strains using a broad-host-range plasmid, best with a long 5'-UTR. Gluconobacter oxydans strain NBRC12528 DELTAadhA::KmR is transformed by triparental mating using Escherichia coli HB101 harboring pRK2013 as the helper strain, Gluconobacter frateurii strain SEI46 (DELTAadhAB) is transformed with the same plasmids by electroporation. Change of the initiation codon to ATG does not improve QDH activity but results in expression levels similar to those achieved with the wild-type plasmid | Gluconobacter oxydans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | transmembrane protein | Gluconobacter oxydans | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
quinate + pyrroloquinoline quinone | Gluconobacter oxydans | - |
3-dehydroquinate + pyrroloquinoline quinol | - |
r | |
quinate + pyrroloquinoline quinone | Gluconobacter oxydans NBRC3293 | - |
3-dehydroquinate + pyrroloquinoline quinol | - |
r | |
quinate + pyrroloquinoline quinone | Gluconobacter oxydans NBRC3244 | - |
3-dehydroquinate + pyrroloquinoline quinol | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gluconobacter oxydans | A0A2Z5U248 | - |
- |
Gluconobacter oxydans | A0A2Z5U421 | - |
- |
Gluconobacter oxydans NBRC3244 | A0A2Z5U421 | - |
- |
Gluconobacter oxydans NBRC3293 | A0A2Z5U248 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from cell membranes by dilution in 10 mM Tris-HCl, pH 7.5, 1 mM CaCl2, and 1% w/v DDM at the final protein concentration of 10 mg/ml followed by incubation for 30 min at 4°C with gentle mixing and ultracentrifugation at 100000 × g for 30 min at 4°C. The resultant supernatant containing the solubilized membranes is resuspended with the same volume of 10 mM Tris-HCl, pH 7.5, and 1 mM CaCl2. The enzyme is solublized from membranes and purified by anion exchange chromatography, dialysis, and hydroxyapatite chromatography | Gluconobacter oxydans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm | Gluconobacter oxydans | ? | - |
- |
|
additional information | QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm | Gluconobacter oxydans NBRC3293 | ? | - |
- |
|
additional information | QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm | Gluconobacter oxydans NBRC3244 | ? | - |
- |
|
quinate + pyrroloquinoline quinone | - |
Gluconobacter oxydans | 3-dehydroquinate + pyrroloquinoline quinol | - |
r | |
quinate + pyrroloquinoline quinone | - |
Gluconobacter oxydans NBRC3293 | 3-dehydroquinate + pyrroloquinoline quinol | - |
r | |
quinate + pyrroloquinoline quinone | - |
Gluconobacter oxydans NBRC3244 | 3-dehydroquinate + pyrroloquinoline quinol | - |
r |
Subunits | Comment | Organism |
---|---|---|
? | x * 88600, about, sequence calculation, x * 100000, recombinant enzyme, SDS-PAGE | Gluconobacter oxydans |
More | prediction of secondary structure of the mRNA | Gluconobacter oxydans |
Synonyms | Comment | Organism |
---|---|---|
PQQ-dependent dehydrogenase | - |
Gluconobacter oxydans |
pyrroloquinoline quinone-dependent dehydrogenase | - |
Gluconobacter oxydans |
QDH | - |
Gluconobacter oxydans |
quiA | - |
Gluconobacter oxydans |
quinoprotein quinate 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 |
---|---|---|---|
6 | - |
assay at | Gluconobacter oxydans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | PQQ-dependent dehydrogenase | Gluconobacter oxydans |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview | Gluconobacter oxydans |
evolution | phylogenetic distribution of QDH with in the membrane-bound, PQQ-dependent proteins of the publicly available Gluconobacter genomes, overview. The genetic sequence of the QDH of NBRC3292 is identical to that of NBRC3244, while the QDH of NBRC3293 is different in 7 amino acids from that of NBRC3244 | Gluconobacter oxydans |
physiological function | Gluconobacter oxydans produces 3-dehydroquinate by oxidation of quinate through a reaction catalyzed by the quinate dehydrogenase (QDH), membrane-bound, pyrroloquinoline quinone (PQQ)-dependent dehydrogenase | Gluconobacter oxydans |