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2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
2-keto-L-gluconic acid + NADH + H+
L-idonate + NAD+
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
2-keto-L-gulonate + NADPH
L-idonate + NADP+
2-oxo-D-gluconate + NADH + H+
D-gluconate + NAD+
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
2-oxo-L-gulonate + NADH + H+
L-idonate + NAD+
-
-
-
r
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
acetaldehyde + NADPH + H+
ethanol + NADP+
-
poor substrate
-
-
?
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
glyoxal + NADPH
?
-
reduction at 33% the rate of 2-ketogluconate reduction
-
-
?
glyoxylate + NADPH
glycolate + NADP+
-
reduction at 350% the rate of 2-ketogluconate reduction
-
?
hydroxypyruvate + NADPH
2,3-dihydroxypropanoate + NADP+
-
reduction at 733% the rate of 2-keto-gluconate reduction
-
?
L-idonate + NAD+
2-oxo-L-gulonate + NADH + H+
-
-
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
L-idonate + NADP+
2-oxo-L-gulonate + NADPH + H+
pyruvate + NADPH + H+
lactate + NADP+
-
reduction at 7% the rate of 2-ketogluconate reduction
-
?
additional information
?
-
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
Brevibacterium ketosoreductum
-
-
-
ir
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
-
-
ir
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
acetic acid bacteria
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
acetic acid bacteria
-
2-keto-D-gluconate, part of non-phosphorylative pathway of carbohydrates predominantly in acetic acid bacteria
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
i.e. 2-keto-D-gluconate, best substrate for Acetobacter ascendens and Gluconobacter
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
i.e. 2-keto-D-gluconate, best substrate for Acetobacter ascendens and Gluconobacter
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
strongly preferred reaction of Acetobacter enzyme
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
equal reaction rate of reduction of 2-ketogluconate and oxidation of gluconate with Gluconobacter enzyme
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
strongly preferred reaction of Acetobacter enzyme
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum
-
11.8% of activity with 2,5-diketo-D-gluconate
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
11.8% of activity with 2,5-diketo-D-gluconate
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
i.e. 2-keto-D-gluconate, best substrate for Acetobacter ascendens and Gluconobacter
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
reverse reaction at the same rate by Gluconobacter enzyme
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
i.e. 2-keto-D-gluconate, best substrate for Acetobacter ascendens and Gluconobacter
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
reverse reaction at the same rate by Gluconobacter enzyme
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
?
2-keto-L-gluconic acid + NADH + H+
L-idonate + NAD+
-
-
-
-
?
2-keto-L-gluconic acid + NADH + H+
L-idonate + NAD+
-
-
-
-
?
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
-
-
-
-
?
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
-
-
-
-
?
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
-
-
-
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
third best substrate
-
-
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
-
-
-
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
betst substrate
-
-
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
Brevibacterium ketosoreductum
-
10.8% of activity with 2,5-diketo-D-gluconate
-
?
2-keto-L-gulonate + NADPH
L-idonate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
10.8% of activity with 2,5-diketo-D-gluconate
-
?
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
-
-
?
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
third best substrate
-
-
r
2-keto-L-gulonate + NADPH
L-idonate + NADP+
-
third best substrate
-
-
r
2-oxo-D-gluconate + NADH + H+
D-gluconate + NAD+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
-
-
?
2-oxo-D-gluconate + NADH + H+
D-gluconate + NAD+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
-
-
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
-
-
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
-
-
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
-
-
-
r
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
-
-
-
r
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
-
-
-
r
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
-
-
-
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
-
-
-
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
poor substrate
-
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
poor substrate
-
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
poor substrate
-
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
poor substrate
-
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
?
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
?
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
-
-
r
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
-
-
r
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
-
-
r
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
-
-
r
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
third best substrate
-
r
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
-
third best substrate
-
r
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
the large subunit is the catalytically active enzyme part, high substrate and regiospecificity
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
the large subunit is the catalytically active enzyme part, high substrate and regiospecificity
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
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
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
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
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
the ability of CHA0 to acidify its environment is largely determined by its ability to produce gluconic acid from glucose
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
the ability of CHA0 to acidify its environment is largely determined by its ability to produce gluconic acid from glucose
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
?
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
-
-
-
?
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
-
-
-
?
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
-
-
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
-
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
poor substrate
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
-
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
poor substrate
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
best substrate
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
-
best substrate
-
?
L-idonate + NADP+
2-oxo-L-gulonate + NADPH + H+
-
-
-
r
L-idonate + NADP+
2-oxo-L-gulonate + NADPH + H+
-
-
-
r
L-idonate + NADP+
2-oxo-L-gulonate + NADPH + H+
-
-
-
r
additional information
?
-
-
no substrates are: 6-phospho-D-gluconate, D-mannonate, D-arabonate
-
-
?
additional information
?
-
-
D-xylonate, D-glucose, D-fructose, L-sorbose, 5-keto-D-fructose, D-sorbitol, glycerol
-
-
?
additional information
?
-
-
no substrates are: 6-phospho-D-gluconate, D-mannonate, D-arabonate
-
-
?
additional information
?
-
-
no substrates are: 6-phospho-D-gluconate, D-mannonate, D-arabonate
-
-
?
additional information
?
-
-
no substrates are: 6-phospho-D-gluconate, D-mannonate, D-arabonate
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
no activity on other sugars and sugar acids
-
-
-
additional information
?
-
-
no activity on other sugars and sugar acids
-
-
-
additional information
?
-
no activity on other sugars and sugar acids
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
additional information
?
-
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
Brevibacterium ketosoreductum
-
-
-
ir
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
-
-
ir
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
acetic acid bacteria
-
2-keto-D-gluconate, part of non-phosphorylative pathway of carbohydrates predominantly in acetic acid bacteria
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
Brevibacterium ketosoreductum ATCC 21914
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
-
-
-
?
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
reverse reaction at the same rate by Gluconobacter enzyme
-
r
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
-
reverse reaction at the same rate by Gluconobacter enzyme
-
r
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
-
-
-
-
?
2-keto-L-gluconic acid + NADPH + H+
L-idonate + NADP+
-
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
-
-
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
-
-
-
?
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
?
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
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.
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.
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.
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.
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.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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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
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metabolism
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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
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physiological function
deletion of the gluC gene results in a phenotype of no growth on D-glucuronate
physiological function
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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
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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
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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
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physiological function
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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
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physiological function
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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
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physiological function
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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
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additional information
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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
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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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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
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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
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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
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additional information
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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
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additional information
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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
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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
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additional information
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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
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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
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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
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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
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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
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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
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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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