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Information on EC 1.1.1.264 - L-idonate 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.264
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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
1.1.1.264 L-idonate 5-dehydrogenase
IUBMB Comments
The enzyme from the bacterium Escherichia coli is specific for 5-dehydro-D-gluconate. cf. EC 1.1.1.366, L-idonate 5-dehydrogenase (NAD+).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.1.1.264
- grape
- berry
-
tartaric
- 5-keto-d-gluconate
- vinifera
-
vitis
-
wine
showSynonyms
l-idndh, l-idonate 5-dehydrogenase, l-idonate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.1.1.128
-
-
formerly
-
GluE
idonate 5-dehydrogenase
-
-
-
-
L-IdnDH
L-idonate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-idonate + NAD(P)+ = 5-dehydro-D-gluconate + NAD(P)H + H+
The enzyme from E. coli cannot oxidize D-gluconate to form 5-dehydrogluconate, a reaction that is catalysed by EC 1.1.1.69, gluconate 5-dehydrogenase
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-idonate:NAD(P)+ oxidoreductase
The enzyme from the bacterium Escherichia coli is specific for 5-dehydro-D-gluconate. cf. EC 1.1.1.366, L-idonate 5-dehydrogenase (NAD+).
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CAS REGISTRY NUMBER
COMMENTARY
211737-68-7
-
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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-gluconate + NADH + H+
L-idonate + NAD+
-
Substrates: -
Products: -
Products: -
?
5-keto-D-fructose + NADP+
? + NADPH
-
Substrates: low activity
Products: -
Products: -
?
L-idonate + NAD(P)+
5-dehydrogluconate + NAD(P)H
Substrates: specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme is part of the D-glucuronic acid catabolism
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme has a strict requirement for NAD+/NADH
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme is part of the D-glucuronic acid catabolism
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme has a strict requirement for NAD+/NADH
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme is part of the D-glucuronic acid catabolism
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme has a strict requirement for NAD+/NADH
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: i.e. 5-keto-D-gluconic acid
Products: i.e. 5-keto-D-gluconic acid
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: highly specific for L-idonate
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
Gluconobacter gluconicus
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: i.e. 5-keto-D-gluconic acid
Products: i.e. 5-keto-D-gluconic acid
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
Substrates: the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
Substrates: -
Products: i.e. 5-keto-D-gluconic acid
Products: i.e. 5-keto-D-gluconic acid
r
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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
L-idonate + NAD(P)+
5-dehydrogluconate + NAD(P)H
Substrates: specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme is part of the D-glucuronic acid catabolism
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme is part of the D-glucuronic acid catabolism
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: the enzyme is part of the D-glucuronic acid catabolism
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: highly specific for L-idonate
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
Gluconobacter gluconicus
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: -
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: role in the control of the intracellular concentration of gluconate
Products: -
Products: -
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
Substrates: the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
Products: -
Products: -
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
Substrates: the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.4
5-Dehydro-D-gluconate
-
pH 7, temperature not specified in the publication
8.4
5-Dehydro-D-gluconate
-
pH 8, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.2
5-Dehydro-D-gluconate
-
pH 7, temperature not specified in the publication
7.2
5-Dehydro-D-gluconate
-
pH 8, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.857
5-Dehydro-D-gluconate
-
pH 7, 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
5.4
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
induction of enzyme synthesis by L-idonate containing culture medium
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
physiological function
-
GluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism
physiological function
-
GluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism
-
physiological function
-
GluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism
-
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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). IDND_ECOLI
Escherichia coli (strain K12)
343
0
37147
Swiss-Prot
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly unstable, 75% loss of activity within a few days, stabilizing agents during purification: D-gluconate, 5-keto-D-gluconate
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3)
recombinant enzyme from Escherichia coli strain BL21(DE3)
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene 1029130, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
gene 1029130, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
-
gene 1029130, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
-
gene 1029130, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bausch, C.; Peekhaus, N.; Utz, C.; Blais, T.; Murray, E.; Lowary, T.; Conway, T.
Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonate acid catabolism in Escherichia coli
J. Bacteriol.
180
3704-3710
1998
Escherichia coli (P39346), Escherichia coli
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, Frateuria aurantia, Gluconacetobacter liquefaciens, Gluconobacter albidus, Gluconobacter cerinus, Gluconobacter gluconicus, Gluconobacter oxydans, Gluconobacter roseus, Gluconobacter sphaericus
-
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
Takagi, Y.
A new enzyme, 5-ketoglucono-idono-reductase
Agric. Biol. Chem.
26
719-720
1962
Fusarium sp.
-
brenda
DeBolt, S.; Cook, D.R.; Ford, C.M.
L-tartaric acid synthesis from vitamin C in higher plants
Proc. Natl. Acad. Sci. USA
103
5608-5613
2006
Ampelopsis glandulosa var. brevipedunculata, no activity in Ampelopsis aconitifolia, Vitis californica, Vitis vinifera (Q1PSI9)
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, Aspergillus niger ATCC 1015
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.264)
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