Any feedback?
Information on EC 1.1.1.264 - L-idonate 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.264Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.264 L-idonate 5-dehydrogenaseIUBMB 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+).
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
l-idndh, l-idonate dehydrogenase, l-idonate 5-dehydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.1.1.128
-
-
formerly
-
GluE
idonate 5-dehydrogenase
-
-
-
-
L-IdnDH
L-idonate dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
211737-68-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-idonate + NAD(P)+
5-dehydrogluconate + NAD(P)H
specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate
-
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme is part of the D-glucuronic acid catabolism
-
-
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme has a strict requirement for NAD+/NADH
-
-
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme is part of the D-glucuronic acid catabolism
-
-
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme has a strict requirement for NAD+/NADH
-
-
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme is part of the D-glucuronic acid catabolism
-
-
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme has a strict requirement for NAD+/NADH
-
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
-
i.e. 5-keto-D-gluconic acid
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
-
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
highly specific for L-idonate
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
Gluconobacter gluconicus
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
-
i.e. 5-keto-D-gluconic acid
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
-
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
i.e. 5-keto-D-gluconic acid
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-idonate + NAD(P)+
5-dehydrogluconate + NAD(P)H
specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate
-
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme is part of the D-glucuronic acid catabolism
-
-
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme is part of the D-glucuronic acid catabolism
-
-
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
the enzyme is part of the D-glucuronic acid catabolism
-
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
-
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
highly specific for L-idonate
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
Gluconobacter gluconicus
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
role in the control of the intracellular concentration of gluconate
-
?
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
-
the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
-
-
r
L-idonate + NADP+
5-dehydro-D-gluconate + NADPH
the enzyme is involved in the biosynthesis of L-tartaric acid from ascorbic acid, pathway overview
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.4
5-Dehydro-D-gluconate
-
pH 8, temperature not specified in the publication
8.4
5-Dehydro-D-gluconate
-
pH 7, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.2
5-Dehydro-D-gluconate
-
pH 8, temperature not specified in the publication
7.2
5-Dehydro-D-gluconate
-
pH 7, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
induction of enzyme synthesis by L-idonate containing culture medium
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Show AA Sequence and Transmembrane Helices (672 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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3)
recombinant enzyme from Escherichia coli strain BL21(DE3)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, Gluconobacter oxydans, Gluconobacter albidus, Gluconobacter cerinus, Gluconobacter gluconicus, Gluconacetobacter liquefaciens, 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
Vitis californica, Ampelopsis glandulosa var. brevipedunculata, no activity in Ampelopsis aconitifolia, 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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.264)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media