Literature summary for 1.1.5.8 extracted from

Yakushi, T.; Komatsu, K.; Matsutani, M.; Kataoka, N.; Vangnai, A.S.; Toyama, H.; Adachi, O.; Matsushita, K.
Improved heterologous expression of the membrane-bound quinoprotein quinate dehydrogenase from Gluconobacter oxydans (2018), Protein Expr. Purif., 145, 100-107 .

Cloned(Commentary)

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

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

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	transmembrane protein	Gluconobacter oxydans	16020	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
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

Organism	UniProt	Comment	Textmining
Gluconobacter oxydans	A0A2Z5U248	-	-
Gluconobacter oxydans	A0A2Z5U421	-	-
Gluconobacter oxydans NBRC3244	A0A2Z5U421	-	-
Gluconobacter oxydans NBRC3293	A0A2Z5U248	-	-

Purification (Commentary)

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

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 and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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

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

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

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	assay at	Gluconobacter oxydans

Cofactor

Cofactor	Comment	Organism	Structure
pyrroloquinoline quinone	PQQ-dependent dehydrogenase	Gluconobacter oxydans

General Information

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