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Information on EC 1.1.1.366 - L-idonate 5-dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.366
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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
1.1.1.366 L-idonate 5-dehydrogenase (NAD+)
IUBMB Comments
Involved in the catabolism of ascorbate (vitamin C) to tartrate. No activity is observed with NADP+ (cf. EC 1.1.1.264, L-idonate 5-dehydrogenase).
The enzyme appears in viruses and cellular organisms
showSynonyms
GluE, L-IdnDH, L-idonate 5-dehydrogenase, L-idonate dehydrogenase, LidnDH, NAD+ requiring L-idonate 5-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GluE
L-IdnDH
L-idonate 5-dehydrogenase
L-idonate dehydrogenase
NAD+ requiring L-idonate 5-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-idonate + NAD+ = 5-dehydro-D-gluconate + NADH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-idonate:NAD+ oxidoreductase
Involved in the catabolism of ascorbate (vitamin C) to tartrate. No activity is observed with NADP+ (cf. EC 1.1.1.264, L-idonate 5-dehydrogenase).
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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: -
r
sorbitol + NAD+
?
-
Substrates: when sorbitol is tested as a substrate, NAD+ reduction occurs but at a very low rate
Products: -
Products: -
r
additional information
?
-
-
Substrates: no activity with NADPH and NADP+
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
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
5-dehydro-D-gluconate + NADH + H+
L-idonate + NAD+
-
Substrates: -
Products: -
Products: -
r
sorbitol + NAD+
?
-
Substrates: when sorbitol is tested as a substrate, NAD+ reduction occurs but at a very low rate
Products: -
Products: -
r
additional information
?
-
-
Substrates: no activity with NADPH and NADP+
Products: -
Products: -
?
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-idonate + NAD+
5-dehydro-D-gluconate + NADH + H+
Substrates: -
Products: -
Products: -
?
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COFACTOR
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 8.0, 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 8.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.86
5-Dehydro-D-gluconate
-
pH 8.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
grape berries from regions Changli (CL) and Gaotai (GT)in eastern and western China,respectively. Some genes required for carbohydrate metabolism, such as hexose transporter, L-idonate dehydrogenase, and phosphoenolpyruvate carboxylase, are significantly upregulated in the CL berries in relation to the GT berries, which positively correlated with the sugar and organic acid accumulations
brenda
high expression level in full bloom, almost no transcript of the enzyme in mature berries
brenda
-
high expression level in full bloom, almost no transcript of the enzyme in mature berries
-
brenda
-
high expression level in full bloom, almost no transcript of the enzyme in mature berries
-
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
enzyme LidnDH catalyzes the conversion of L-idonate to 5-keto D-gluconic acid in plant and is proposed to be a rate-limiting step in biosynthesis of tartaric acid from ascorbic acid
additional information
cultivar Cabernet Sauvignon transcriptome analysis dependent on regional parameters of six different samples, overview. Two unigenes encoding L-idonate dehydrogenase (LidnDH) are detected from the assembled transcriptome. One is expressed higher in Changli region berries than in Gaotai region berries at E-L 31 stage,while the other is expressed higher at E-L 38 stage in Gaotai region berries
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 (EC 1.1.1.264). The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE. 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 (EC 1.1.1.264). The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE. 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 (EC 1.1.1.264). The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE. The genes coding for these two enzymes are clustered and share the same bidirectional promoter
-
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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_VITVI
366
0
39466
Swiss-Prot
other Location (Reliability: 1)
A0A5B7AVX9_DAVIN
376
0
40565
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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 gluE deletion mutant strain, phenotype, overview. The gluE deletion in Aspergillus niger causes a phenotype with reduced growth and ceased D-glcUA consumption
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 gluE deletion mutant strain, phenotype, overview. The gluE deletion in Aspergillus niger causes a phenotype with reduced growth and ceased D-glcUA consumption
-
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 gluE deletion mutant strain, phenotype, overview. The gluE deletion in Aspergillus niger causes a phenotype with reduced growth and ceased D-glcUA consumption
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gluE, clustered with gene gluD, 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
-
gene LidnDH, DNA library construction from a single pool of six samples, DNA sequence determination and comparisons, quantitative real-time PCR enzyme expression analysis in different regional samples of cv. Cabernet Sauvignon berries
IdnDh gene, quantitative expression analysis on transcriptional and translational levels in fruits of different stages
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 vinifera
brenda
Wen, Y.Q.; Li, J.M.; Zhang, Z.Z.; Zhang, Y.F.; Pan, Q.H.
Antibody preparation, gene expression and subcellular localization of L-idonate dehydrogenase in grape berry
Biosci. Biotechnol. Biochem.
74
2413-2417
2010
Vitis vinifera (Q1PSI9), Vitis vinifera Cabernet Sauvignon (Q1PSI9), Vitis vinifera Syrah (Q1PSI9)
brenda
Sun, R.; He, F.; Lan, Y.; Xing, R.; Liu, R.; Pan, Q.; Wang, J.; Duan, C.
Transcriptome comparison of Cabernet Sauvignon grape berries from two regions with distinct climate
J. Plant Physiol.
178
43-54
2015
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, Aspergillus niger CBS 113.46
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.366)
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Release 2023.1 (January 2023)
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