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Information on EC 1.1.1.69 - gluconate 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.69
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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
1.1.1.69 gluconate 5-dehydrogenase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.1.1.69
-
gluconobacter
- oxydans
- suboxydans
-
2-keto-d-gluconic
- dehydrogenases
- food industry
-
undesired
- l-sorbose
- tetramer
-
oxidoreduction
- synthesis
- analysis
showSynonyms
ga5dh, gluconate 5-dehydrogenase, 5-keto-d-gluconate 5-reductase, gluconate-5-dehydrogenase, gluconate:nadp 5-oxidoreductase, nadph-dependent 5-keto-d-gluconate reductase, 5kga reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-keto-D-gluconate 5-reductase
5-keto-D-gluconate reductase
5-ketogluconate 5-reductase
-
-
-
-
5-ketogluconate reductase
-
-
-
-
5KGR
dehydrogenase, gluconate 5-
-
-
-
-
GA5DH
gluconate-5-dehydrogenase
gluconate:NADP 5-oxidoreductase
-
-
-
-
GluF
GNO
-
-
-
-
NADPH-dependent 5-keto-D-gluconate reductase
reductase, 5-ketogluconate 5-
-
-
-
-
5-keto-D-gluconate 5-reductase
-
-
-
-
5-keto-D-gluconate reductase
-
-
-
-
5KGR
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-gluconate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-gluconate:NAD(P)+ 5-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-70-0
-
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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
5-dehydro-D-fructose + NADPH
D-fructose + NADP+
-
Substrates: 23% of the activity with 5-dehydro-D-gluconate
Products: -
Products: -
?
5-keto D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
D-glucono-delta-lactone + NADP+
?
-
Substrates: 14% of the activity with D-gluconate
Products: -
Products: -
?
D-mannitol + NAD+
? + NADH
Substrates: 74% of activity with D-sorbitol
Products: -
Products: -
?
glycerol + NAD+
? + NADH
Substrates: 138% of activity with D-sorbitol
Products: -
Products: -
?
ribitol + NAD+
? + NADH
Substrates: 66% of activity with D-sorbitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: production of 5-keto D-gluconate from D-gluconate
Products: -
Products: -
?
2,3-butanediol + NAD+
? + NADH
Substrates: 169% of activity with D-sorbitol
Products: -
Products: -
?
2,3-butanediol + NAD+
? + NADH
Substrates: 169% of activity with D-sorbitol
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH
D-gluconate + NAD+
-
Substrates: reaction proceeds twice as fast with NADH as with NADPH
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH
D-gluconate + NAD+
-
Substrates: no reaction with NADH
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH
D-gluconate + NAD+
-
Substrates: reaction proceeds twice as fast with NADH as with NADPH
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: inducible enzyme
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
r
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: the rate of D-gluconate oxidation is about 60% of the rate of 5-keto-D-gluconate reduction
Products: -
Products: -
r
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
r
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: the suggested physiological role of the enzyme is to reduce 5-dehydro-D-gluconate to D-gluconate to supply a carbon source and regenerate NADP+
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: maximum enzyme formation at the end of the exponential growth, in the decreasing growth phase, about 65% of the maximum enzyme activity remains
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: inducible enzyme
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: enzyme is involved in gluconate metabolism
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: enzyme is involved in gluconate metabolism
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
Substrates: -
Products: -
Products: -
r
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
Substrates: -
Products: -
Products: -
r
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
D-arabitol + NAD+
? + NADH
Substrates: 130% of activity with D-sorbitol
Products: -
Products: -
?
D-arabitol + NAD+
? + NADH
Substrates: 130% of activity with D-sorbitol
Products: -
Products: -
?
D-fructose + NADPH
5-dehydro-D-fructose + NADP+
-
Substrates: 42% of the activity with 5-dehydro-D-gluconate
Products: -
Products: -
?
D-fructose + NADPH
5-dehydro-D-fructose + NADP+
-
Substrates: 10% of the activity with 5-dehydrydro-D-gluconate
Products: -
Products: -
?
D-gluconate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-gluconate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
Acetobacter acetigenus
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
Gluconobacter gluconicus
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: the rate of D-gluconate oxidation is about 60% of the rate of 5-keto-D-gluconate reduction
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH + H+
Substrates: -
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH + H+
Substrates: -
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-gluconic acid + NAD+
? + NADH
Substrates: 8% of activity with D-sorbitol
Products: -
Products: -
?
D-gluconic acid + NAD+
? + NADH
Substrates: 8% of activity with D-sorbitol
Products: -
Products: -
?
D-glucose + ?
5-keto-D-gluconic acid + ?
-
Substrates: -
Products: -
Products: -
?
D-glucose + ?
5-keto-D-gluconic acid + ?
-
Substrates: -
Products: -
Products: -
?
D-sorbitol + NAD+
? + NADH
Substrates: -
Products: -
Products: -
?
meso-erytritol + NAD+
? + NADH
Substrates: 143% of activity with D-sorbitol
Products: -
Products: -
?
meso-erytritol + NAD+
? + NADH
Substrates: 143% of activity with D-sorbitol
Products: -
Products: -
?
sorbitol + NAD+
? + NADH
-
Substrates: -
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
additional information
?
-
-
Substrates: production of 5-keto D-gluconate from D-gluconate
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADH + H+
D-gluconate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: inducible enzyme
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: the suggested physiological role of the enzyme is to reduce 5-dehydro-D-gluconate to D-gluconate to supply a carbon source and regenerate NADP+
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: maximum enzyme formation at the end of the exponential growth, in the decreasing growth phase, about 65% of the maximum enzyme activity remains
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: inducible enzyme
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: enzyme is involved in gluconate metabolism
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
Substrates: enzyme is involved in gluconate metabolism
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
5-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
Substrates: -
Products: -
Products: -
?
D-gluconate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-gluconate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-gluconate + NADP+
5-dehydro-D-gluconate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
5-Dehydro-D-gluconate
pH 7, temperature not specified in the publication
3.2
5-Dehydro-D-gluconate
pH 7.0, temperature not specified in the publication
8.4
D-gluconate
pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2 - 3.7
5-Dehydro-D-gluconate
pH 7, temperature not specified in the publication
2 - 3.7
5-Dehydro-D-gluconate
pH 7.0, temperature not specified in the publication
2.6
D-gluconate
pH 8.0, 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
10 - 11
6 - 7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
-
pH 4.5: about 70% of maximal activity, pH 8.5: about 60% of maximal activity, reduction of 5-dehydro-D-gluconate
8 - 12
-
pH 8.0: about 30% of maximal activity, pH 12.0: 35% of maximal activity, oxidation of D-gluconate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50
-
reduction of 5-dehydro-D-gluconate and oxidation of D-gluconate
50
-
reduction of 5-dehydro-D-gluconate and oxidation of D-gluconate
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NBRC3172, also Gluconobacter suboxydans IFO12528, genetically identical with Gluconobacter oxydans 621H
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
malfunction
the disruption of the gene, gluF, by CRISPR/Cas9 in the filamentous fungus Aspergillus niger results in a strain unable to catabolise D-glucuronate
malfunction
-
the disruption of the gene, gluF, by CRISPR/Cas9 in the filamentous fungus Aspergillus niger results in a strain unable to catabolise D-glucuronate
-
metabolism
the enzyme is involved in the pathway for D-glucuronate catabolism in fungi
metabolism
-
the enzyme is involved in the pathway for D-glucuronate catabolism in fungi
-
physiological function
-
the enzyme prevents the formation of ectopic Z rings during Streptococcus suis cell division and plays a role in septum constriction
physiological function
gene disruption results in a strain unable to catabolise D-glucuronate. A pathway for D-glucuronate catabolism is suggested with the intermediates L-gulonate, 2-keto-L-gulonate, L-idonate, 5-keto-D-gluconate, D-gluconate and D-gluconate-6-phosphate
physiological function
-
the enzyme prevents the formation of ectopic Z rings during Streptococcus suis cell division and plays a role in septum constriction
-
physiological function
-
gene disruption results in a strain unable to catabolise D-glucuronate. A pathway for D-glucuronate catabolism is suggested with the intermediates L-gulonate, 2-keto-L-gulonate, L-idonate, 5-keto-D-gluconate, D-gluconate and D-gluconate-6-phosphate
-
Show AA Sequence and Transmembrane Helices (556 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method, crystal structure solved at 2.1 A resolution. The crystal belongs to the monoclinic system, with space group P1 and unit-cell parameters a: 55.42, b: 55.48, c: 79.16 A, alpha: 100.51°, beta: 105.66°, gamma: 97.99°
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
5 min, in presence of D-gluconate or 5-dehydro-D-gluconate, even at 0.0001 mg/ml protein
additional information
additional information
-
thermal stability is enhanced by addition of either D-gluconate or 5-keto-D-gluconate, or both
additional information
-
thermal stability is enhanced by addition of either D-gluconate or 5-keto-D-gluconate, or both
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
75% loss of activity within a few days unless either D-gluconate or 5-dehydro-D-gluconate is added during storage or purification
-
unstable to dialysis in a cold room, in presence of sulfhydryl compounds, EDTA, sucrose and/or glycerol
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM phosphate buffer, pH 6.0, no added 2-mercaptoethanol, fully stable for at least 3 days
-
5°C, pH 7.5, 0.01 M potassium phosphate buffer, 3 d, complete loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as fusion protein with a N-terminal His6 tag in Escherichia coli strain BL21 (DE3)
A4VVQ2
expressed in Escherichia coli BL21(DE3), expression levels vary from colony to colony, cells showing high enzyme expression tend to show less growth, expression system appears to be unstable as expression level decreases when subcultured for several times, best expression results with freshly transformed cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
synthesis
-
strain overexpressing enzyme plus Escherichia coli transhydrogenase sthA, enhanced accumulation of 5-ketoD-gluconate, precursor of L-(+)-tartaric acid
food industry
-
production of 5-keto-D-gluconic acid that can be converted effectively into L-(+)-tartaric acid
food industry
-
production of 5-keto-D-gluconic acid that can be converted effectively into L-(+)-tartaric acid
-
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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
brenda
Chiyonobu, T.; Shinagawa, E.; Adachi, O.; Ameyama, M.
Distribution of 2-ketogluconate reductase and 5-ketogluconate reductase in acetic acid bacteria
Agric. Biol. Chem.
39
2425-2427
1975
Acetobacter aceti, Acetobacter acetigenus, Acetobacter ascendens, Acetobacter orleanensis, Acetobacter pasteurianus, Frateuria aurantia, Gluconacetobacter liquefaciens, Gluconobacter albidus, Gluconobacter cerinus, Gluconobacter gluconicus, Gluconobacter oxydans, Gluconobacter roseus, Gluconobacter sphaericus, Komagataeibacter xylinus
-
brenda
Adachi, O.; Shinagawa, E.; Matsushita, K.; Ameyama, M.
Crystallization and properties of 5-keto-D-gluconate reductase from Gluconobacter suboxydans
Agric. Biol. Chem.
43
75-83
1979
Gluconobacter oxydans
-
brenda
Ameyama, M.; Adachi, O.
5-keto-D-Gluconate reductase from Gluconobacter suboxydans
Methods Enzymol.
89
198-202
1982
Gluconobacter oxydans
-
brenda
De Ley, J.
5-Ketogluconic acid reductase
Methods Enzymol.
9
200-203
1966
Gluconobacter oxydans, Klebsiella sp., Escherichia coli
-
brenda
Ameyama, M.; Chiyonobu, T.; Adachi, O.
Purification and properties of 5-ketogluconate reductase from Gluconobacter liquefaciens
Agric. Biol. Chem.
38
1377-1382
1974
Gluconacetobacter liquefaciens
-
brenda
Klasen, R.; Bringer-Meyer, S.; Sahm, H.
Investigation of 5-ketogluconate formation by Gluconobacter oxydans
DECHEMA Biotechnol. Conf.
5
109-112
1992
Gluconobacter oxydans
-
brenda
Herrmann, U.; Merfort, M.; Jeude, M.; Bringer-Meyer, S.; Sahm, H.
Biotransformation of glucose to 5-keto-D-gluconic acid by recombinant Gluconobacter oxydans DSM 2343
Appl. Microbiol. Biotechnol.
64
86-90
2004
Gluconobacter oxydans
brenda
Salusjarvi, T.; Povelainen, M.; Hvorslev, N.; Eneyskaya, E.V.; Kulminskaya, A.A.; Shabalin, K.A.; Neustroev, K.N.; Kalkkinen, N.; Miasnikov, A.N.
Cloning of a gluconate/polyol dehydrogenase gene from Gluconobacter suboxydans IFO 12528, characterisation of the enzyme and its use for the production of 5-ketogluconate in a recombinant Escherichia coli strain
Appl. Microbiol. Biotechnol.
65
306-314
2004
Gluconobacter oxydans (Q70JN9), Gluconobacter oxydans (Q70JP0), Gluconobacter oxydans, Gluconobacter oxydans IFO 12528 (Q70JN9), Gluconobacter oxydans IFO 12528 (Q70JP0)
brenda
Elfari, M.; Ha, S.W.; Bremus, C.; Merfort, M.; Khodaverdi, V.; Herrmann, U.; Sahm, H.; Gorisch, H.
A Gluconobacter oxydans mutant converting glucose almost quantitatively to 5-keto-D-gluconic acid
Appl. Microbiol. Biotechnol.
66
668-674
2005
Gluconobacter oxydans
brenda
Merford, M.; Herrmann, U.; Bringer-Meyer, S.; Sahm, H.
High-yield 5-keto-D-gluconic acid formation is mediated by soluble and membrane-bound gluconate-5-dehydrogenases of Gluconobacter oxydans
Appl. Microbiol. Biotechnol.
73
443-4051
2006
Gluconobacter oxydans
brenda
Merford, M.; Herrmann, U.; Ha, S.W.; Elfari, M.; Ha, S.W.; Bringer-Meyer, S.; Goerisch, H.; Sahm, H.
Modification of the membrane-bound glucose oxidation system in Gluconobacter oxydans significantly increases gluconate and 5-keto-D-gluconic acid accumulation
J. Biotechnol.
1
556-563
2006
Gluconobacter oxydans, Gluconobacter oxydans DSM 2343 (ATCC 621H)
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
brenda
Zhang, Q.; Peng, H.; Gao, F.; Liu, Y.; Cheng, H.; Thompson, J.; Gao, G.F.
Structural insight into the catalytic mechanism of gluconate 5-dehydrogenase from Streptococcus suis: Crystal structures of the substrate-free and quaternary complex enzymes
Protein Sci.
18
294-303
2009
Streptococcus suis (A4VVQ2), Streptococcus suis
brenda
Chen, M.; Li, Y.; Li, S.; Tang, L.; Zheng, J.; An, Q.
Genomic identification of nitrogen-fixing Klebsiella variicola, K. pneumoniae and K. quasipneumoniae
J. Basic Microbiol.
56
78-84
2016
Klebsiella pneumoniae subsp. pneumoniae, Klebsiella pneumoniae subsp. pneumoniae DSM 30104T, Klebsiella pneumoniae subsp. rhinoscleromatis, Klebsiella pneumoniae subsp. rhinoscleromatis ATCC 13884T, Klebsiella quasipneumoniae subsp. quasipneumoniae, Klebsiella quasipneumoniae subsp. quasipneumoniae 01A030T, Klebsiella quasipneumoniae subsp. similipneumoniae, Klebsiella quasipneumoniae subsp. similipneumoniae 07A044T, Klebsiella variicola, Klebsiella variicola DSM 15968T
brenda
Shi, Z.; Xuan, C.; Han, H.; Cheng, X.; Wang, J.; Feng, Y.; Srinivas, S.; Lu, G.; Gao, G.F.
Gluconate 5-dehydrogenase (Ga5DH) participates in Streptococcus suis cell division
Protein Cell
5
761-769
2014
Streptococcus suis, Streptococcus suis 05ZYH33
brenda
Kuivanen, J.; Richard, P.
NADPH-dependent 5-keto-D-gluconate reductase is a part of the fungal pathway for D-glucuronate catabolism
FEBS Lett.
592
71-77
2018
Aspergillus niger (G3XRE5), Aspergillus niger, Aspergillus niger ATCC 1015 (G3XRE5)
brenda
Tian, D.; Fu, X.; Cao, W.; Yuan, H.
Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum
Acta Crystallogr. Sect. F
76
228-234
2020
Lentibacter algarum (A0A1H3NGY9), Lentibacter algarum
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.69)
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