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Information on EC 1.1.1.215 - gluconate 2-dehydrogenase and Organism(s) Gluconobacter oxydans and UniProt Accession Q5FTU6

for references in articles please use BRENDA:EC1.1.1.215
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IUBMB Comments
Also acts on L-idonate, D-galactonate and D-xylonate.
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This record set is specific for:
Gluconobacter oxydans
UNIPROT: Q5FTU6
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The taxonomic range for the selected organisms is: Gluconobacter oxydans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gluconate dehydrogenase, fad-gadh, ga2dh, gluconate-2-dehydrogenase, 2-ketogluconate reductase, 2-ketoaldonate reductase, l-2-hydroxyacid dehydrogenase, 2-keto-l-gulonate reductase, 2-ketogluconate dehydrogenase, gox0417, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-keto-D-gluconate reductase
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-
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2-ketoaldonate reductase
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-
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2-ketogluconate reductase
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-
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2KR
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-
-
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gluconate-2-dehydrogenase
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reductase, 2-ketogluconate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
D-gluconate:NADP+ oxidoreductase
Also acts on L-idonate, D-galactonate and D-xylonate.
CAS REGISTRY NUMBER
COMMENTARY hide
68417-42-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-D-gluconate + NADH + H+
D-gluconate + NAD+
show the reaction diagram
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
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-
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
show the reaction diagram
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
show the reaction diagram
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-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
show the reaction diagram
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-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
show the reaction diagram
2-keto-L-gulonate + NADPH
L-idonate + NADP+
show the reaction diagram
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third best substrate
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-
r
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
show the reaction diagram
-
-
-
?
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
show the reaction diagram
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third best substrate
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r
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
show the reaction diagram
-
-
-
?
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
show the reaction diagram
-
-
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
show the reaction diagram
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best substrate
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
show the reaction diagram
-
-
-
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
show the reaction diagram
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
show the reaction diagram
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-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
show the reaction diagram
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reverse reaction at the same rate by Gluconobacter enzyme
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r
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
show the reaction diagram
-
-
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
bound by the middle subunit
FAD
enzyme bound to the large subunit
NADP+
additional information
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no activity with NADH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no metal requirement
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hg2+
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complete inhibition
sulfhydryl reagents
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strong
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.16
2-oxo-D-gluconate
pH 7.0, 25°C
0.051
NADH
pH 7.0, 25°C
0.01
NADPH
below 0.01 mM, pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48.2
2-oxo-D-gluconate
pH 7.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.34
2-oxo-D-gluconate
pH 7.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
reduction of 2-ketogluconate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme is located on the periplasmic side of the cytoplasmic membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33200
6 * 33200, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 33200, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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crude and crystallized, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol at 5°C
286275
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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stable for 5 min, enhanced by the addition of substrate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
5°C, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, overexpression of wild-type and expression of start codon mutated enzyme in Escherichia coli strain DH5alpha
expression in Escherichia coli
gene ga2dh, recombinant overexpression of the enzyme in Gluconobacter oxydans strain DSM2003 under the control of three promoters, PtufB, Pga2dh or Pghp0169, respectively. Recombinant strain Gluconobacter oxydans_tufB_ga2dh shows a similar growth rate to that of the control strain and displays the highest specific productivity of 2-dehydro-D-gluconate from D-gluconate, which is increased nearly twofold compared with that of the control strain during batch biotransformation, method optimization
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
about 2fold upregulation in presence of 7.85 mM H2O2, and upregulation in presence of some lignocellulosic degradation compounds of corn stover hydrolysate
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ameyama, M.; Adachi, O.
2-keto-D-Gluconate reductase from acetic acid bacteria
Methods Enzymol.
89
203-210
1982
Acetobacter ascendens, Gluconobacter oxydans, Acetobacter pasteurianus, Gluconacetobacter liquefaciens
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Manually annotated by BRENDA team
Saichana, I.; Ano, Y.; Adachi, O.; Matsushita, K.; Toyama, H.
Preparation of enzymes required for enzymatic quantification of 5-keto-D-gluconate and 2-keto-D-gluconate
Biosci. Biotechnol. Biochem.
71
2478-2486
2007
Gluconobacter oxydans (Q5FTU6), Gluconobacter oxydans 621H (Q5FTU6), Gluconobacter oxydans 621H
Manually annotated by BRENDA team
Rauch, B.; Pahlke, J.; Schweiger, P.; Deppenmeier, U.
Characterization of enzymes involved in the central metabolism of Gluconobacter oxydans
Appl. Microbiol. Biotechnol.
88
711-718
2010
Gluconobacter oxydans (Q5FTU6), Gluconobacter oxydans, Gluconobacter oxydans 621H (Q5FTU6)
Manually annotated by BRENDA team
Li, K.; Mao, X.; Liu, L.; Lin, J.; Sun, M.; Wei, D.; Yang, S.
Overexpression of membrane-bound gluconate-2-dehydrogenase to enhance the production of 2-keto-D-gluconic acid by Gluconobacter oxydans
Microb. Cell Fact.
15
121
2016
Gluconobacter oxydans (Q5FRK5), Gluconobacter oxydans, Gluconobacter oxydans 621H (Q5FRK5)
Manually annotated by BRENDA team
Zhou, X.; Shen, Y.; Xu, Y.; Balan, V.
Directing cell catalysis of glucose to 2-keto-D-gluconic acid using Gluconobacter oxydans NL71
Process Biochem.
94
365-369
2020
Gluconobacter oxydans, Gluconobacter oxydans NL71
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Manually annotated by BRENDA team