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Information on EC 1.1.1.215 - gluconate 2-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.215
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.215 gluconate 2-dehydrogenase
IUBMB Comments
Also acts on L-idonate, D-galactonate and D-xylonate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.1.1.215
-
2-keto-d-gluconic
- gluconobacter
- oxydans
- 5-keto-d-gluconate
- gluconokinase
- 6-phosphogluconate
-
entner-doudoroff
- l-idonate
- cypripedii
-
2.7.1.12
- synthesis
- medicine
showSynonyms
gluconate dehydrogenase, fad-gadh, ga2dh, gluconate-2-dehydrogenase, 2-ketoaldonate reductase, l-2-hydroxyacid dehydrogenase, 2-keto-l-gulonate reductase, 2-ketogluconate reductase, 2-ketogluconate dehydrogenase, gox0417, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-HDH
2-keto-D-gluconate reductase
-
-
-
-
2-keto-D-gluconate-yielding D-gluconate dehydrogenase
2-keto-L-gulonate reductase
2-ketoaldonate reductase
-
-
-
-
2-ketogluconate dehydrogenase
2-ketogluconate reductase
-
-
-
-
2KGA reductase
2KGR
2KR
-
-
-
-
FAD-GADH
GA2DH
GAD
GADH
gluconate dehydrogenase
gluconate-2-dehydrogenase
GluD
Gox0417
GOX1230
HDH
L-2-hydroxyacid dehydrogenase
NADPH requiring 2-keto-L-gulonate reductase
reductase, 2-ketogluconate
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-gluconate + NADP+ = 2-dehydro-D-gluconate + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
ketogluconate metabolism
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SYSTEMATIC NAME
IUBMB Comments
D-gluconate:NADP+ oxidoreductase
Also acts on L-idonate, D-galactonate and D-xylonate.
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CAS REGISTRY NUMBER
COMMENTARY
68417-42-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxo-L-gulonate + NADH + H+
L-idonate + NAD+
Substrates: -
Products: -
Products: -
r
acetaldehyde + NADPH + H+
ethanol + NADP+
-
Substrates: poor substrate
Products: -
Products: -
?
glyoxal + NADPH
?
-
Substrates: reduction at 33% the rate of 2-ketogluconate reduction
Products: -
Products: -
?
glyoxylate + NADPH
glycolate + NADP+
-
Substrates: reduction at 350% the rate of 2-ketogluconate reduction
Products: -
Products: -
?
hydroxypyruvate + NADPH
2,3-dihydroxypropanoate + NADP+
-
Substrates: reduction at 733% the rate of 2-keto-gluconate reduction
Products: -
Products: -
?
L-idonate + NAD+
2-oxo-L-gulonate + NADH + H+
Substrates: -
Products: -
Products: -
?
pyruvate + NADPH + H+
lactate + NADP+
-
Substrates: reduction at 7% the rate of 2-ketogluconate reduction
Products: -
Products: -
?
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
Brevibacterium ketosoreductum
-
Substrates: -
Products: -
Products: -
ir
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
Substrates: -
Products: -
Products: -
ir
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
acetic acid bacteria
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
acetic acid bacteria
-
Substrates: 2-keto-D-gluconate, part of non-phosphorylative pathway of carbohydrates predominantly in acetic acid bacteria
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: i.e. 2-keto-D-gluconate, best substrate for Acetobacter ascendens and Gluconobacter
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: strongly preferred reaction of Acetobacter enzyme
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: equal reaction rate of reduction of 2-ketogluconate and oxidation of gluconate with Gluconobacter enzyme
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: strongly preferred reaction of Acetobacter enzyme
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum
-
Substrates: 11.8% of activity with 2,5-diketo-D-gluconate
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
Substrates: 11.8% of activity with 2,5-diketo-D-gluconate
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: i.e. 2-keto-D-gluconate, best substrate for Acetobacter ascendens and Gluconobacter
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: reverse reaction at the same rate by Gluconobacter enzyme
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: i.e. 2-keto-D-gluconate, best substrate for Acetobacter ascendens and Gluconobacter
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: reverse reaction at the same rate by Gluconobacter enzyme
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-keto-L-gluconic acid + NADH + H+
L-idonate + NAD+
-
Substrates: -
Products: -
Products: -
?
2-keto-L-gluconic acid + NADH + H+
L-idonate + NAD+
-
Substrates: -
Products: -
Products: -
?
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
Substrates: third best substrate
Products: -
Products: -
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
Substrates: betst substrate
Products: -
Products: -
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
Brevibacterium ketosoreductum
-
Substrates: 10.8% of activity with 2,5-diketo-D-gluconate
Products: -
Products: -
?
2-keto-L-gulonate + NADPH
L-idonate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
Substrates: 10.8% of activity with 2,5-diketo-D-gluconate
Products: -
Products: -
?
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
Substrates: third best substrate
Products: -
Products: -
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
Substrates: third best substrate
Products: -
Products: -
r
2-oxo-D-gluconate + NADH + H+
D-gluconate + NAD+
Substrates: enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
Products: -
Products: -
?
2-oxo-D-gluconate + NADH + H+
D-gluconate + NAD+
Substrates: enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
Products: -
Products: -
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
Substrates: -
Products: -
Products: -
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
Substrates: enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
Products: -
Products: -
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
Substrates: -
Products: -
Products: -
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
Substrates: enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
Products: -
Products: -
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
Substrates: -
Products: -
Products: -
r
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
Substrates: -
Products: -
Products: -
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
Substrates: -
Products: -
Products: -
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: poor substrate
Products: -
Products: -
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: poor substrate
Products: -
Products: -
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
Substrates: -
Products: -
Products: -
r
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
Substrates: -
Products: -
Products: -
r
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
Substrates: third best substrate
Products: -
Products: -
r
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
Substrates: third best substrate
Products: -
Products: -
r
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: the large subunit is the catalytically active enzyme part, high substrate and regiospecificity
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: the large subunit is the catalytically active enzyme part, high substrate and regiospecificity
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
Substrates: wild-type exhibits gluconate-dependent respiration. Genes cj0414 and cj0415, orthologous to GADH, are co-transcribed. Campylobacter jejuni 81176 does not use gluconate compounds as sole carbon sources. GADH plays a minor role in mouse colonization
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
Substrates: wild-type exhibits gluconate-dependent respiration. Genes cj0414 and cj0415, orthologous to GADH, are co-transcribed. Campylobacter jejuni 81176 does not use gluconate compounds as sole carbon sources. GADH plays a minor role in mouse colonization
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
Substrates: the ability of CHA0 to acidify its environment is largely determined by its ability to produce gluconic acid from glucose
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
Substrates: the ability of CHA0 to acidify its environment is largely determined by its ability to produce gluconic acid from glucose
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
Pseudomonas plecoglossicida JUIM01
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
Substrates: -
Products: -
Products: -
?
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
-
Substrates: -
Products: -
Products: -
?
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
-
Substrates: -
Products: -
Products: -
?
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
-
Substrates: -
Products: -
Products: -
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
Substrates: -
Products: -
Products: -
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
Substrates: poor substrate
Products: -
Products: -
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
Substrates: -
Products: -
Products: -
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
Substrates: poor substrate
Products: -
Products: -
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
Substrates: best substrate
Products: -
Products: -
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
Substrates: best substrate
Products: -
Products: -
?
L-idonate + NADP+
2-oxo-L-gulonate + NADPH + H+
Substrates: -
Products: -
Products: -
r
L-idonate + NADP+
2-oxo-L-gulonate + NADPH + H+
Substrates: -
Products: -
Products: -
r
L-idonate + NADP+
2-oxo-L-gulonate + NADPH + H+
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: no substrates are: 6-phospho-D-gluconate, D-mannonate, D-arabonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-xylonate, D-glucose, D-fructose, L-sorbose, 5-keto-D-fructose, D-sorbitol, glycerol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates are: 6-phospho-D-gluconate, D-mannonate, D-arabonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates are: 6-phospho-D-gluconate, D-mannonate, D-arabonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates are: 6-phospho-D-gluconate, D-mannonate, D-arabonate
Products: -
Products: -
?
additional information
?
-
Substrates: for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
Products: -
Products: -
?
additional information
?
-
-
Substrates: for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
Products: -
Products: -
?
additional information
?
-
Substrates: for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
Products: -
Products: -
?
additional information
?
-
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
Substrates: no activity on other sugars and sugar acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity on other sugars and sugar acids
Products: -
Products: -
?
additional information
?
-
Pseudomonas plecoglossicida JUIM01
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
Substrates: no activity on other sugars and sugar acids
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
Brevibacterium ketosoreductum
-
Substrates: -
Products: -
Products: -
ir
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
Substrates: -
Products: -
Products: -
ir
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
acetic acid bacteria
-
Substrates: 2-keto-D-gluconate, part of non-phosphorylative pathway of carbohydrates predominantly in acetic acid bacteria
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: reverse reaction at the same rate by Gluconobacter enzyme
Products: -
Products: -
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: reverse reaction at the same rate by Gluconobacter enzyme
Products: -
Products: -
r
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
-
Substrates: -
Products: -
Products: -
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
Substrates: -
Products: -
Products: -
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
Substrates: -
Products: -
Products: -
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
Substrates: -
Products: -
Products: -
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
Products: -
Products: -
?
additional information
?
-
-
Substrates: for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
Products: -
Products: -
?
additional information
?
-
Substrates: for large-scale production of 2-dehydro-D-gluconate, the cells require for formation of 2-dehydro-D-gluconate from D-gluconate oxygen as the final acceptor of electrons formed during the oxidation ofD -gluconate
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the larger enzyme domain is responsible for binding the cofactor and contains a conserved [GXGXXG (X17) D] motif that is characteristic of the NAD(P)H/NAD(P)+-binding region. It consists of residues 103-287, forming a seven-stranded parallel beta-sheet flanked by seven alpha-helices
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
not inhibitory: EDTA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression and activity of cj0414 and cj0415 are higher at 42°C than at 37°C
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Sarcoma
Sheep gene mapping: additional DNA markers included (CASB, CASK, LALBA, IGF-1 and AMH).
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.6
2-keto-L-gluconic acid
-
recombinant His6-tagged enzyme, pH and temperature not specified in the publication
25.3
2-oxo-L-gulonate
pH 7, temperature not specified in the publication
12.6
L-Idonate
pH 8, temperature not specified in the publication
0.11
NADH
-
recombinant His6-tagged enzyme, pH and temperature not specified in the publication
0.05
NADPH
-
recombinant His6-tagged enzyme, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.4
2-oxo-L-gulonate
pH 7, temperature not specified in the publication
1.1
L-Idonate
pH 8, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.85
2-dehydro-D-gluconate
pH 8.0, temperature not specified in the publication
0.846
2-oxo-L-gulonate
pH 7, temperature not specified in the publication
0.087
L-Idonate
pH 8, temperature not specified in the publication
0.087
L-Idonate
pH 7.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
12
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 12
-
about half-maximal activity at pH 10 and 12, oxidation of gluconate
10.8 - 12.5
-
about half-maximal activity at pH 10.8 and 12.5, oxidation of gluconate
4.5 - 8.5
-
about half-maximal activity at pH 4.5 and 8.5, reduction of ketogluconate
5 - 9.2
-
about half-maximal activity at pH 5.0 and 9.2, reduction of ketogluconate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the large subunit is encoded by gene gndL, the small subunit by gene gndS, and the cytochrome C subunit by gene gndC; gene gndL encoding the large subunit of the enzyme
UniProt
brenda
the large subunit is encoded by gene gndL, the small subunit by gene gndS, and the cytochrome C subunit by gene gndC; gene gndL encoding the large subunit of the enzyme
UniProt
brenda
A0A2H4PJM1 i.e gamma subunit, A0A2H4PJM2 i.e. FAD containing subunit, A0A2H4PJM7 i.e. cytochrome c subunit
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
UniProt
brenda
Pseudomonas plecoglossicida JUIM01
A0A2H4PJM1 i.e gamma subunit, A0A2H4PJM2 i.e. FAD containing subunit, A0A2H4PJM7 i.e. cytochrome c subunit
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme is located on the periplasmic side of the cytoplasmic membrane
brenda
-
the enzyme is located on the periplasmic side of the cytoplasmic membrane
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
gluD deletion results in accumulation of 2-keto-L-gulonate in the liquid cultivation, while the gluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism
malfunction
-
gluD deletion results in accumulation of 2-keto-L-gulonate in the liquid cultivation, while the gluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism
-
malfunction
-
gluD deletion results in accumulation of 2-keto-L-gulonate in the liquid cultivation, while the gluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism
-
metabolism
in the filamentous fungus Aspergillus niger, the enzymes that are known to be part of the D-glucuronic acid catabolism pathway are the NADPH requiring D-glucuronic acid reductase forming L-gulonate and the NADH requiring 2-keto-L-gulonate reductase that forms L-idonate. With the aid of RNA sequencing two more enzymes of the pathway are identified. The first is a NADPH requiring 2-keto-L-gulonate reductase that forms L-idonate, GluD. The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE (EC 1.1.1.366). The genes coding for these two enzymes are clustered and share the same bidirectional promoter
metabolism
-
in the filamentous fungus Aspergillus niger, the enzymes that are known to be part of the D-glucuronic acid catabolism pathway are the NADPH requiring D-glucuronic acid reductase forming L-gulonate and the NADH requiring 2-keto-L-gulonate reductase that forms L-idonate. With the aid of RNA sequencing two more enzymes of the pathway are identified. The first is a NADPH requiring 2-keto-L-gulonate reductase that forms L-idonate, GluD. The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE (EC 1.1.1.366). The genes coding for these two enzymes are clustered and share the same bidirectional promoter
-
metabolism
-
in the filamentous fungus Aspergillus niger, the enzymes that are known to be part of the D-glucuronic acid catabolism pathway are the NADPH requiring D-glucuronic acid reductase forming L-gulonate and the NADH requiring 2-keto-L-gulonate reductase that forms L-idonate. With the aid of RNA sequencing two more enzymes of the pathway are identified. The first is a NADPH requiring 2-keto-L-gulonate reductase that forms L-idonate, GluD. The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE (EC 1.1.1.366). The genes coding for these two enzymes are clustered and share the same bidirectional promoter
-
physiological function
deletion of the gluC gene results in a phenotype of no growth on D-glucuronate
physiological function
-
Gluconobacter oxydans NBRC3293 produces 2,5-dioxo-D-gluconate from D-glucose via D-gluconate and 2-keto-D-gluconate, with accumulation of the product in the culture medium, the efficiency of 2,5-diketo-D-gluconate production is unsatisfactory because there is a large amount of residual D-gluconate at the end of the biotransformation process. Heterologous overexpression of the kgdSLC genes in a mutant strain of Gluconobacter japonicus NBRC3271 engineered to produce 2-dehydro-D-gluconate efficiently from a mixture of D-glucose and D-gluconate, results in a mutant strain that consumes almost all of the starting materials (D-glucose and D-gluconate) to produce 2,5-dioxo-D-gluconate quantitatively as a seemingly unique metabolite
physiological function
-
the enzyme catalyzes the bioconversion of 2-dehydro-L-gulonic acid to L-idonate, which plays a negative role in the manufacture of vitamin C. The primary biochemical function of HDH from Ketogulonicigenium vulgare is C=O bond oxidation-reduction, cf. EC 1.1.1.272
physiological function
a GluD deletion mutant does not show reduced growth when cultivated on agar plate with D-glucuronate as sole carbon source. In the liquid cultivation on D-glucuronate, 2-oxo-L-gulonate accumulates in the medium after D-glucuronate is consumed
physiological function
-
a GluD deletion mutant does not show reduced growth when cultivated on agar plate with D-glucuronate as sole carbon source. In the liquid cultivation on D-glucuronate, 2-oxo-L-gulonate accumulates in the medium after D-glucuronate is consumed
-
physiological function
-
the enzyme catalyzes the bioconversion of 2-dehydro-L-gulonic acid to L-idonate, which plays a negative role in the manufacture of vitamin C. The primary biochemical function of HDH from Ketogulonicigenium vulgare is C=O bond oxidation-reduction, cf. EC 1.1.1.272
-
physiological function
-
Gluconobacter oxydans NBRC3293 produces 2,5-dioxo-D-gluconate from D-glucose via D-gluconate and 2-keto-D-gluconate, with accumulation of the product in the culture medium, the efficiency of 2,5-diketo-D-gluconate production is unsatisfactory because there is a large amount of residual D-gluconate at the end of the biotransformation process. Heterologous overexpression of the kgdSLC genes in a mutant strain of Gluconobacter japonicus NBRC3271 engineered to produce 2-dehydro-D-gluconate efficiently from a mixture of D-glucose and D-gluconate, results in a mutant strain that consumes almost all of the starting materials (D-glucose and D-gluconate) to produce 2,5-dioxo-D-gluconate quantitatively as a seemingly unique metabolite
-
physiological function
-
a GluD deletion mutant does not show reduced growth when cultivated on agar plate with D-glucuronate as sole carbon source. In the liquid cultivation on D-glucuronate, 2-oxo-L-gulonate accumulates in the medium after D-glucuronate is consumed
-
additional information
-
the amino acid residues Arg234, Glu263 and His 279 form the active site of enzyme HDH. Residues Arg234, Ala210, Thr211, and Arg212, which are located on top of the catalytic triad, act as a size filter to jointly determine the substrate specificity
additional information
-
the amino acid residues Arg234, Glu263 and His 279 form the active site of enzyme HDH. Residues Arg234, Ala210, Thr211, and Arg212, which are located on top of the catalytic triad, act as a size filter to jointly determine the substrate specificity
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A4PIB0_9PROT
593
0
65284
TrEMBL
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
trimer
additional information
dimer
Brevibacterium ketosoreductum ATCC 21914
-
2 * 35000, SDS-PAGE
-
additional information
-
the enzyme shows a structure consisting of two-compact domains separated by a deep active cleft. This typical topology is conserved in other 2-HDH. The smaller domain is the substrate binding domain or catalytic domain, which is formed from N-terminal residues 2-102 and C-terminal residues 288-317. It is folded into a five-stranded parallel beta-sheet flanked by five alpha-helices, forming a modified Rossmann topology. The larger domain is responsible for binding the cofactor and contains a conserved [GXGXXG (X17) D] motif that is characteristic of the NAD(P)H/NAD(P)+-binding region. It consists of residues 103-287, forming a seven-stranded parallel beta-sheet flanked by seven alpha-helices. A two-stranded hinge connects the two domains showing flexibility during catalysis
additional information
-
the enzyme shows a structure consisting of two-compact domains separated by a deep active cleft. This typical topology is conserved in other 2-HDH. The smaller domain is the substrate binding domain or catalytic domain, which is formed from N-terminal residues 2-102 and C-terminal residues 288-317. It is folded into a five-stranded parallel beta-sheet flanked by five alpha-helices, forming a modified Rossmann topology. The larger domain is responsible for binding the cofactor and contains a conserved [GXGXXG (X17) D] motif that is characteristic of the NAD(P)H/NAD(P)+-binding region. It consists of residues 103-287, forming a seven-stranded parallel beta-sheet flanked by seven alpha-helices. A two-stranded hinge connects the two domains showing flexibility during catalysis
-
additional information
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
enzyme consists of a gamma subunit, a flavoprotein subunit, and a cytochrome c subunit with molecular masses of about 27, 65, and 47 kDa, respectively
additional information
-
enzyme consists of a gamma subunit, a flavoprotein subunit, and a cytochrome c subunit with molecular masses of about 27, 65, and 47 kDa, respectively
additional information
Pseudomonas plecoglossicida JUIM01
-
enzyme consists of a gamma subunit, a flavoprotein subunit, and a cytochrome c subunit with molecular masses of about 27, 65, and 47 kDa, respectively
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 30 mg/ml protein in 25 mM Tris/HCl, pH 8.0, 0.3 M NaCl, and 1 mM dithiothreitol, with 0.001 ml of reservoir solution containing 23% w/v PEG 3350, 0.2 M MgCl2, and 0.1 M HEPES, pH 7.0, and equilibration against 0.1 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.64 A resolution, molecular replacement and modeling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
identification of a gene cluster encoding NADPH-dependent, L-idonate forming, 2-keto-L-gulonate reductase and NAD+-dependent L-idonate 5-dehydrogenase which forms 5-keto-D-gluconate. These genes are involved in the fungal D-glcUA catabolism and the reaction catalyzed by the latter enzyme is a direct continuation for the previously identified reaction by the action of GluC. Generation of a gene gluD deletion mutant strain, phenotype, overview. Deletion of gluD does not result in reduced or no growth on D-glcUA as sole carbon source, but it results in a phenotype of accumulating 2-keto-L-gulonate when cultivating on D-glcUA
additional information
-
identification of a gene cluster encoding NADPH-dependent, L-idonate forming, 2-keto-L-gulonate reductase and NAD+-dependent L-idonate 5-dehydrogenase which forms 5-keto-D-gluconate. These genes are involved in the fungal D-glcUA catabolism and the reaction catalyzed by the latter enzyme is a direct continuation for the previously identified reaction by the action of GluC. Generation of a gene gluD deletion mutant strain, phenotype, overview. Deletion of gluD does not result in reduced or no growth on D-glcUA as sole carbon source, but it results in a phenotype of accumulating 2-keto-L-gulonate when cultivating on D-glcUA
additional information
-
identification of a gene cluster encoding NADPH-dependent, L-idonate forming, 2-keto-L-gulonate reductase and NAD+-dependent L-idonate 5-dehydrogenase which forms 5-keto-D-gluconate. These genes are involved in the fungal D-glcUA catabolism and the reaction catalyzed by the latter enzyme is a direct continuation for the previously identified reaction by the action of GluC. Generation of a gene gluD deletion mutant strain, phenotype, overview. Deletion of gluD does not result in reduced or no growth on D-glcUA as sole carbon source, but it results in a phenotype of accumulating 2-keto-L-gulonate when cultivating on D-glcUA
-
additional information
-
identification of a gene cluster encoding NADPH-dependent, L-idonate forming, 2-keto-L-gulonate reductase and NAD+-dependent L-idonate 5-dehydrogenase which forms 5-keto-D-gluconate. These genes are involved in the fungal D-glcUA catabolism and the reaction catalyzed by the latter enzyme is a direct continuation for the previously identified reaction by the action of GluC. Generation of a gene gluD deletion mutant strain, phenotype, overview. Deletion of gluD does not result in reduced or no growth on D-glcUA as sole carbon source, but it results in a phenotype of accumulating 2-keto-L-gulonate when cultivating on D-glcUA
-
additional information
-
cj0414 and cj0415 mutants lack GADH activity at either temperature. Cj0415 mutant does not exhibit gluconate-dependent respiration. Cj0415 mutant is defective in chicken colonization, but exhibits only a minor colonization defect in mice
additional information
-
cj0414 and cj0415 mutants lack GADH activity at either temperature. Cj0415 mutant does not exhibit gluconate-dependent respiration. Cj0415 mutant is defective in chicken colonization, but exhibits only a minor colonization defect in mice
-
additional information
-
a mutant strain of Gluconobacter japonicus NBRC3271 is engineered to produce 2-dehydro-D-gluconate efficiently from a mixture of D-glucose and D-gluconate
additional information
-
a mutant strain of Gluconobacter japonicus NBRC3271 is engineered to produce 2-dehydro-D-gluconate efficiently from a mixture of D-glucose and D-gluconate
-
additional information
development of an efficient bacterial strain of Gluconobacter oxydans_tufB_ga2dh for the production of 2-dehydro-D-gluconate by overexpressing the ga2dh gene in Gluconobacter oxydans. Supply of sufficient oxygen enhances the positive effect of gene overexpression on 2-dehydro-D-gluconate production. Gluconobacter oxydans_tufB_ga2dh is a competitive species for use in 2-dehydro-D-gluconate production. Transgenic strains, evaluation and optimization, detailed overview
additional information
-
development of an efficient bacterial strain of Gluconobacter oxydans_tufB_ga2dh for the production of 2-dehydro-D-gluconate by overexpressing the ga2dh gene in Gluconobacter oxydans. Supply of sufficient oxygen enhances the positive effect of gene overexpression on 2-dehydro-D-gluconate production. Gluconobacter oxydans_tufB_ga2dh is a competitive species for use in 2-dehydro-D-gluconate production. Transgenic strains, evaluation and optimization, detailed overview
additional information
-
development of an efficient bacterial strain of Gluconobacter oxydans_tufB_ga2dh for the production of 2-dehydro-D-gluconate by overexpressing the ga2dh gene in Gluconobacter oxydans. Supply of sufficient oxygen enhances the positive effect of gene overexpression on 2-dehydro-D-gluconate production. Gluconobacter oxydans_tufB_ga2dh is a competitive species for use in 2-dehydro-D-gluconate production. Transgenic strains, evaluation and optimization, detailed overview
-
additional information
DELTAgad, and DELTAgcd/DELTAgad mutants are indistinguishable from the wild-type with respect to their growth characteristics and morphologies in liquid or solid nutrient-rich media. In the DELTAgcd mutant, which does not produce gluconic acid, the enhanced production of antifungal compounds is associated with improved biocontrol activity against take-all disease of wheat, caused by Gaeumannomyces graminis var. tritici
additional information
-
DELTAgad, and DELTAgcd/DELTAgad mutants are indistinguishable from the wild-type with respect to their growth characteristics and morphologies in liquid or solid nutrient-rich media. In the DELTAgcd mutant, which does not produce gluconic acid, the enhanced production of antifungal compounds is associated with improved biocontrol activity against take-all disease of wheat, caused by Gaeumannomyces graminis var. tritici
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
Brevibacterium ketosoreductum
-
35% of activity left after incubation at pH 8.4 for 2 h at 30°C, no remaining activity below pH 5.2 or above pH 10.0
6
-
crude and crystallized, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol at 5°C
6
-
stable for a week in the cold, increasing inactivation below and above, stable for a month or more with additional 2-mercaptoethanol
6
-
crude and crystallized, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol at 5°C
6
-
crude and crystallized, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol at 5°C
6
-
crude and crystallized, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol at 5°C
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
70
-
stable for 10 min in the presence of either 2-ketogluconate or gluconate
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-ketogluconate enhances thermal and storage stability even of dilute enzyme solutions, 0.1 mg protein/l
-
gluconate enhances thermal and storage stability even of dilute enzyme solutions, 0.1 mg protein/l
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
Ethanol
hexane
isopentanol
Methanol
Acetone
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
40% v/v, 32% residual activity
Ethanol
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
40% v/v, complete loss of activity
hexane
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
40% v/v, 39% residual activity
isopentanol
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
40% v/v, complete loss of activity
Methanol
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
40% v/v, complete loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable in the presence of sulfhydryl agents and ammonium sulfate
-
5C, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol
ammonium sulfate solution of crystalline enzyme stable for over 2 years
-
5C, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol
-
5C, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol
-
5C, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol
-
5C, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Toyopearl, Phenyl-Toyopearl, Blue-Sepharose, Sephacryl S-200
Brevibacterium ketosoreductum
-
native enzyme 67fold from membranes and bound to FAD by solubilization with 0.1% Triton X-100, anion chromatography, and three steps of hydrophobic interaction chromatography
native enzyme, via ultrasonification and ultracentrifugation, phase separation, ammonium sulfate precipitation, and DEAE-Sepharose and hydroxyapatite chromatography
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity and anion exchange chromatography, followed by gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant large subunits
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
gene gluD, clustered with gene gluE, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strains ATCC 90845 and modified CEN.PK2, subcloning in Escherichia coli strain TOP10
mutagenized cj0414 and cj0415 alleles are introduced into Campylobacter jejuni 81-176
-
recombinant overexpression of C-terminally His6-tagged enzyme in Escherichia coli
-
expression in Escherichia coli
A0A2H4PJM1; A0A2H4PJM2; A0A2H4PJM7
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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
about 2fold upregulation in presence of 7.85 mM H2O2, and upregulation in presence of some lignocellulosic degradation compounds of corn stover hydrolysate
-
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
LITERATURE
medicine
synthesis
medicine
-
ability of Campylobacter jejuni to use gluconate as an electron donor via GADH activity is an important metabolic characteristic that is required for full colonization of avian but not mammalian hosts
medicine
-
ability of Campylobacter jejuni to use gluconate as an electron donor via GADH activity is an important metabolic characteristic that is required for full colonization of avian but not mammalian hosts
-
synthesis
ga2dh-overexpressing strain Gluconobacter oxydans_tufB_ga2dh is a useful species for use in 2-dehydro-D-gluconate production
synthesis
-
pulse addition of hydrogen peroxide to synthetic media is beneficial to improve the conversion rate of glucose to 2-oxo-gluconate by 1.47fold
synthesis
-
ga2dh-overexpressing strain Gluconobacter oxydans_tufB_ga2dh is a useful species for use in 2-dehydro-D-gluconate production
-
synthesis
-
pulse addition of hydrogen peroxide to synthetic media is beneficial to improve the conversion rate of glucose to 2-oxo-gluconate by 1.47fold
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pitt, D.; Mosley, M.J.
Enzymes of gluconate metabolism and glycolysis in Penicillium notatum
Antonie van Leeuwenhoek
51
353-364
1985
Penicillium chrysogenum, Penicillium chrysogenum Westling
brenda
Chiyonobu, T.; Shinagawa, E.; Adachi, O.; Ameyama, M.
Purification, crystallization and properties of 2-ketogluconate reductase from Acetobacter rancens
Agric. Biol. Chem.
40
175-184
1976
Acetobacter pasteurianus
-
brenda
Adachi, O.; Chiyonobu, T.; Shinagawa, E.; Matsushita, K.; Ameyama, M.
Crystalline 2-ketogluconate reductase from Acetobacter ascendens, the second instance of crystalline enzyme in genus Acetobacter
Agric. Biol. Chem.
42
2057-2062
1978
Acetobacter ascendens
-
brenda
Ameyama, M.; Adachi, O.
2-keto-D-Gluconate reductase from acetic acid bacteria
Methods Enzymol.
89
203-210
1982
Acetobacter pasteurianus, Acetobacter ascendens, Gluconacetobacter liquefaciens, Gluconobacter oxydans
-
brenda
Shinagawa, E.; Chiyonobu, T.; Matsushita, K.; Adachi, O.; Ameyama, M.
Distribution of gluconate dehydrogenase and ketogluconate reductases in aerobic bacteria
Agric. Biol. Chem.
42
1055-1057
1978
acetic acid bacteria, no activity in a number of oxidative or aerobic bacteria
-
brenda
Yum, D-Y.; Bae, S-S.; Pan, J-G.
Purification and characterization of the 2-ketoaldonate reductase from Brevibacterium ketosoreductum ATCC21914
Biosci. Biotechnol. Biochem.
62
154-156
1998
Brevibacterium ketosoreductum
brenda
Yum, D-Y.; Lee, B-Y.; Hahm, D-H.; Pan, J-G.
The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase
J. Bacteriol.
180
5984-5988
1998
Escherichia coli
brenda
Toyama, H.; Furuya, N.; Saichana, I.; Ano, Y.; Adachi, O.; Matsushita, K.
Membrane-bound, 2-keto-D-gluconate-yielding D-gluconate dehydrogenase from Gluconobacter dioxyacetonicus IFO 3271: molecular properties and gene disruption
Appl. Environ. Microbiol.
73
6551-6556
2007
Gluconobacter frateurii (A4PIB0), Gluconobacter frateurii IFO 3271 (A4PIB0)
brenda
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
brenda
De Werra, P.; Pechy-Tarr, M.; Keel, C.; Maurhofer, M.
Role of gluconic acid production in the regulation of biocontrol traits of Pseudomonas fluorescens CHA0
Appl. Environ. Microbiol.
75
4162-4174
2009
Pseudomonas fluorescens (C0LE03), Pseudomonas fluorescens CHA0 (C0LE03)
brenda
Pajaniappan, M.; Hall, J.E.; Cawthraw, S.A.; Newell, D.G.; Gaynor, E.C.; Fields, J.A.; Rathbun, K.M.; Agee, W.A.; Burns, C.M.; Hall, S.J.; Kelly, D.J.; Thompson, S.A.
A temperature-regulated Campylobacter jejuni gluconate dehydrogenase is involved in respiration-dependent energy conservation and chicken colonization
Mol. Microbiol.
68
474-491
2008
Campylobacter jejuni, Campylobacter jejuni 81-176
brenda
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)
brenda
Kataoka, N.; Matsutani, M.; Yakushi, T.; Matsushita, K.
Efficient production of 2,5-diketo-D-gluconate via heterologous expression of 2-ketogluconate dehydrogenase in Gluconobacter japonicus
Appl. Environ. Microbiol.
81
3552-3560
2015
Gluconobacter japonicus, Gluconobacter japonicus NBRC3271
brenda
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)
brenda
Kuivanen, J.; Sugai-Guerios, M.H.; Arvas, M.; Richard, P.
A novel pathway for fungal D-glucuronate catabolism contains an L-idonate forming 2-keto-L-gulonate reductase
Sci. Rep.
6
26329
2016
Aspergillus niger (A0A1D8RK43), Aspergillus niger
brenda
Han, X.; Xiong, X.; Hu, X.; Li, M.; Zhang, W.; Liu, X.
Crystallization and structural analysis of 2-hydroxyacid dehydrogenase from Ketogulonicigenium vulgare
Biotechnol. Lett.
36
295-300
2014
Ketogulonicigenium vulgare, Ketogulonicigenium vulgare Y25
brenda
Wang, D.M.; Sun, L.; Sun, W.J.; Cui, F.J.; Gong, J.S.; Zhang, X.M.; Shi, J.S.; Xu, Z.H.
A membrane-bound gluconate dehydrogenase from 2-keto-D-gluconic acid industrial producing strain Pseudomonas plecoglossicida JUIM01 Purification, characterization, and gene identification
Appl. Biochem. Biotechnol.
188
897-913
2019
Pseudomonas plecoglossicida (A0A2H4PJM1 and A0A2H4PJM2 and A0A2H4PJM7), Pseudomonas plecoglossicida, Pseudomonas plecoglossicida JUIM01 (A0A2H4PJM1 and A0A2H4PJM2 and A0A2H4PJM7)
brenda
Kuivanen, J.; Arvas, M.; Richard, P.
Clustered genes encoding 2-keto-L-gulonate reductase and L-idonate 5-dehydrogenase in the novel fungal D-glucuronic acid pathway
Front. Microbiol.
8
225
2017
Aspergillus niger (A0A1D8RK43), Aspergillus niger, Aspergillus niger ATCC 1015 (A0A1D8RK43), Aspergillus niger CBS 113.46 (A0A1D8RK43)
brenda
Hyskova, V.; Pliskova, V.; Cerveny, V.; Ryslava, H.
NADP-dependent enzymes are involved in response to salt and hypoosmotic stress in cucumber plants
Gen. Physiol. Biophys.
36
247-258
2017
Cucumis sativus
brenda
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
-
brenda
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