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3-OH-benzopyrene + NAD+
?
-
-
-
-
?
5-azido-UDP-glucose + NAD+
5-azido-UDP-glucuronate + NADH + H+
-
-
-
-
?
5-fluorouracil + NAD+
?
-
-
-
-
?
6-azauracil + NAD+
?
-
-
-
-
?
CDP-glucose + NAD+ + H2O
CDP-glucuronate + NADH
CTP-glucose + NAD+
CTP-glucuronate + NADH
Saccharum spp.
-
8% of activity with UDP-glucose
-
-
ir
dTDP-glucose + NAD+ + H2O
dTDP-glucuronate + NADH
-
reaction rate is 16.7% of that with UDPglucose
-
-
?
TDP-glucose + NAD+
TDP-glucuronate + NADH
Saccharum spp.
-
2% of activity with UDP-glucose
-
-
ir
TDP-glucose + NAD+ + H2O
TDP-glucuronate + NADH
UDP-2-deoxy-D-glucose + NAD+ + H2O
UDP-2-deoxy-D-glucuronate + NADH
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
UDP-alpha-D-mannose + 2 NAD+ + H2O
UDP-alpha-D-mannuronate + 2 NADH + 2 H+
UDP-D-galactose + 2 NAD+ + H2O
UDP-alpha-D-galacturonate + 2 NADH + 2 H+
UDP-galactose + NAD+ + H2O
UDP-galacturonate + NADH
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
UDP-glucose + 3-pyridinealdehyde adenine dinucleotide
UDP-glucuronate
-
-
-
-
?
UDP-glucose + deamino adenine dinucleotide + H2O
UDP-glucuronate + ?
UDP-glucose + nicotinamide hypoxanthine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + thionicotinamide adenine dinucleotide + H2O
UDP-glucuronate + ?
UDP-N-acetylglucosamine + NAD+ + H2O
? + NADH
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
additional information
?
-
CDP-glucose + NAD+ + H2O
CDP-glucuronate + NADH
-
reaction rate is 5.5% of that with UDP-glucose
-
-
?
CDP-glucose + NAD+ + H2O
CDP-glucuronate + NADH
-
17% of the reaction rate with UDP-glucose
-
-
?
TDP-glucose + NAD+ + H2O
TDP-glucuronate + NADH
-
reaction rate is 17% of that with UDPglucose
-
-
?
TDP-glucose + NAD+ + H2O
TDP-glucuronate + NADH
38.5% of the rate with UDP-glucose
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
UDP-glucuronic acid is a key precursor in the biosynthesis of glycoconjugates
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
the enzyme is involved in protein N-glycosylation
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
the enzyme is involved in protein N-glycosylation
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
r
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
UDP-glucuronate is a key sugar nucleotide involved in biosynthesis of the plant cell wall
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
UDP-alpha-D-glucuronate is a precursor in the synthesis of many exopolysaccharides
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
UDP-alpha-D-glucuronate is a precursor in the synthesis of many exopolysaccharides
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-alpha-D-mannose + 2 NAD+ + H2O
UDP-alpha-D-mannuronate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-alpha-D-mannose + 2 NAD+ + H2O
UDP-alpha-D-mannuronate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-D-galactose + 2 NAD+ + H2O
UDP-alpha-D-galacturonate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-D-galactose + 2 NAD+ + H2O
UDP-alpha-D-galacturonate + 2 NADH + 2 H+
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
-
-
?
UDP-galactose + NAD+ + H2O
UDP-galacturonate + NADH
11.9% of the rate with UDP-glucose
-
-
?
UDP-galactose + NAD+ + H2O
UDP-galacturonate + NADH
6.4% of the rate with UDP-glucose
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
reversal of reaction cannot be demonstrated
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
recombinant forms Ugd(BCAL2946) and Ugd(BCAM0855) have similar in vitro Ugd activity
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
NADP+, about 1% of activity of NAD+
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
C276 is an active catalytic residue and critically involved in the substrate binding
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
the enzyme has dual specificity with UDP-glucose and ethanol
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
Saccharum spp.
-
-
-
-
ir
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
the enzyme has a crucial role during development of Xenopus laevis. Silencing of UGDH decreases glycosaminoglycan synthesis causing severe embryonic malformations because of defective gastrulation process
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
several different UDPGDH isoenzymes contribute to UDP-glucuronate and hence wall matrix biosynthesis in maize
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
-
UDPGDH-A activity has a more important role than UDPGDH-B in synthesis of UDP-glucuronate
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + deamino adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + deamino adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + thionicotinamide adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-glucose + thionicotinamide adenine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
-
?
UDP-N-acetylglucosamine + NAD+ + H2O
? + NADH
35% of the rate with UDP-glucose
-
-
?
UDP-N-acetylglucosamine + NAD+ + H2O
? + NADH
6.3% of the rate with UDP-glucose
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
first step of a branched pathway leading to plant cell-wall polysaccharides which contain glucuronic and galacturonic acids and the pentoses xylose, arabinose and apiose
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
-
delivers glucuronic acid for the formation of a antiphagocytic polysaccharide capsule that is required for virulence of pathogenic bacteria
-
-
?
additional information
?
-
-
importance of both UDPDH and mshA gene expression for successful light organ colonization in the sepiolid squid Euprymna tasmanica
-
-
?
additional information
?
-
-
no substrate: ADP-glucose, TDP-glucose
-
-
?
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
-
-
?
additional information
?
-
-
no reaction with NADP+
-
-
?
additional information
?
-
-
no activity with glucose
-
-
?
additional information
?
-
-
deamino adenine dinucleotide
-
-
?
additional information
?
-
-
no activity with uridine diphosphoacetylgalactosamine
-
-
?
additional information
?
-
-
no activity with ethyl alcohol
-
-
?
additional information
?
-
-
no activity with alpha-D-glucose-1-phosphate
-
-
?
additional information
?
-
-
no activity with guanosine diphosphomannose
-
-
?
additional information
?
-
-
no activity with uridine diphosphoacetylglucosamine
-
-
?
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia but only the most highly expressed ugd gene, Ugd(BCAL2946), is required for polymyxin B resistance. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia but only the most highly expressed ugd gene, Ugd(BCAL2946), is required for polymyxin B resistance. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia but only the most highly expressed ugd gene, Ugd(BCAL2946), is required for polymyxin B resistance. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. Combined activity of Ugd(BCAL2946) and Ugd(BCAM0855) is essential for the survival of Burkholderia cenocepacia. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
purified Ugd(BCAM2034) shows no in vitro Ugd activity. Expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
purified Ugd(BCAM2034) shows no in vitro Ugd activity. Expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
purified Ugd(BCAM2034) shows no in vitro Ugd activity. Expression of Ugd(BCAL2946) is 5.4- and 135fold greater than that of Ugd(BCAM0855) and Ugd(BCAM2034), respectively. UDP-galactose, UDP-acetylglucosamine and GDP-mannose are not substrates
-
-
?
additional information
?
-
no amide products are found in the presence of added amines. The addition of either ethanolamine, ethanolamine phosphate, serinol, or serinol phosphate has no measurable effect on the catalytic properties
-
-
-
additional information
?
-
no amide products are found in the presence of added amines. The addition of either ethanolamine, ethanolamine phosphate, serinol, or serinol phosphate has no measurable effect on the catalytic properties
-
-
-
additional information
?
-
-
no substrates: UDP-D-galactose, UTP, 5'-UMP and D-galactose
-
-
?
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
-
-
?
additional information
?
-
-
3-pyridinealdehyde adenine dinucleotide
-
-
?
additional information
?
-
-
thionicotinamide adenine dinucleotide
-
-
?
additional information
?
-
-
no activity with GTP-glucose
-
-
?
additional information
?
-
-
no reaction with: 3-pyridinealdehyde deamino adenosine dinucleotide
-
-
?
additional information
?
-
-
deamino adenine dinucleotide
-
-
?
additional information
?
-
-
no activity with ADP-glucose
-
-
?
additional information
?
-
-
no substrate: UDP-galactose, UDP-N-galactosamin, ADP-glucose, GDP-glucose, GDP-mannose
-
-
?
additional information
?
-
enzyme displays hysteresis, observed as a lag in progress curves, and is sensitive to product inhibition during the lag. The inhibition results in a systematic decrease in steady-state velocity and makes the lag appear to have a second-order dependence on enzyme concentration.The lag is in fact due to a substrate and cofactor-induced isomerization of the enzyme. The cofactor binds to the enzyme:substrate complex with negative cooperativity, suggesting that the isomerization may be related to the formation of an asymmetric enzyme complex
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additional information
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enzyme displays hysteresis, observed as a lag in progress curves, and is sensitive to product inhibition during the lag. The inhibition results in a systematic decrease in steady-state velocity and makes the lag appear to have a second-order dependence on enzyme concentration.The lag is in fact due to a substrate and cofactor-induced isomerization of the enzyme. The cofactor binds to the enzyme:substrate complex with negative cooperativity, suggesting that the isomerization may be related to the formation of an asymmetric enzyme complex
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additional information
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the transient capacity to dissociate and reorganize the hydrogen bond network at the interface between dimeric units is an important element of the normal catalytic cycle
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additional information
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no reaction with NADP+
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additional information
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no reaction with ethylnicotinate adenine dinucleotide
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?
additional information
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cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
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?
additional information
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no reaction with alpha-NAD+
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additional information
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no reaction with 3-formylpyridine adenine dinucleotide
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?
additional information
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thionicotinamide adenine dinucleotide
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?
additional information
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no reaction with deamino-NAD+
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?
additional information
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no reaction with 3-propionylpyridine adenine dinucleotide
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additional information
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nicotinamide hypoxanthine dinucleotide
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?
additional information
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no reaction with alpha-NAD+
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?
additional information
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Saccharum spp.
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no substrate: ADP-glucose
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additional information
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the enzyme is also not only able to bind RNA but also acts as a ribonuclease. The ribonucleolytic activity occurs independently of the presence of NAD+ and the RNA binding site does not coincide with the NAD+ binding region, kinetics of interaction between UgdG and RNA, overview. The Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease
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additional information
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the enzyme is also not only able to bind RNA but also acts as a ribonuclease. The ribonucleolytic activity occurs independently of the presence of NAD+ and the RNA binding site does not coincide with the NAD+ binding region, kinetics of interaction between UgdG and RNA, overview. The Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease
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additional information
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the enzyme is also not only able to bind RNA but also acts as a ribonuclease. The ribonucleolytic activity occurs independently of the presence of NAD+ and the RNA binding site does not coincide with the NAD+ binding region, kinetics of interaction between UgdG and RNA, overview. The Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease
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evolution
the enzyme belongs to the the UGDH family of proteins
evolution
the N- and C-terminal domains of UgdG share structural features with ancient mitochondrial ribonucleases named MAR. MARs are present in lower eukaryotic microorganisms, have a Rossmannoid-fold and belong to the isochorismatase superfamily
evolution
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the enzyme belongs to the the UGDH family of proteins
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evolution
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the N- and C-terminal domains of UgdG share structural features with ancient mitochondrial ribonucleases named MAR. MARs are present in lower eukaryotic microorganisms, have a Rossmannoid-fold and belong to the isochorismatase superfamily
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malfunction
Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
malfunction
mutant dimeric species of UGDH have reduced activity in vitro and in supporting hyaluronan production by cultured cells. The purified enzymes reveal a significant decrease in the enzymatic activity of the obligate dimer and hexamer mutants. Both T325A and T325D mutants were significantly less efficient in promoting downstream hyaluronan production by HEK293 cells
malfunction
UGDH protein level in rat osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis
malfunction
UGDH specific siRNAs markedly inhibits UGDH mRNA and protein expression, and leads to an obvious suppression of proteoglycans synthesis in human articular chondrocytes. UGDH protein level in human osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis. Interleukin-1beta inhibits UGDH gene expression through modulating UGDH transregulators and the downstream signaling cascades, including the SAP/JNK and p38 MAPK pathways which might be involved in the proteoglycans loss of osteoarthritis cartilage and contribute to the osteoarthritis pathogenesis
malfunction
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UGDH protein level in rat osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis
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malfunction
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Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
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metabolism
in the Haloferax volcanii archaeal glycosylation pathway, Agl, responsible for the assembly and attachment of an Asn-linked pentasaccharide, enzyme AglM acts as a UDP-glucose dehydrogenase, converting UDP-glucose into UDP-glucuronic acid
metabolism
the enzyme participates in sucrose/polysaccharide metabolism and cell wall biosynthesis
metabolism
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enzyme displays a NAD+-dependent SN2 mechanism. The first oxidation involves the nucleophilic addition of the essential Cys residue. The acceptor of C6-OH of UDP-glucose is an ordered H2O molecule. The second NADH is released after hydrolysis of the thioester intermediate
metabolism
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in the Haloferax volcanii archaeal glycosylation pathway, Agl, responsible for the assembly and attachment of an Asn-linked pentasaccharide, enzyme AglM acts as a UDP-glucose dehydrogenase, converting UDP-glucose into UDP-glucuronic acid
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physiological function
UDP-glucose dehydrogenase is responsible for the NAD-dependent twofold oxidation of UDP-glucose to UDP-glucuronic acid, one of the key components for gellan biosynthesis
physiological function
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UGDH oxidizes UDP-glucose to UDP-glucuronate, an essential precursor for production of hyaluronan, proteoglycans, and xenobiotic glucuronides. High levels of hyaluronan turnover in prostate cancer are correlated with aggressive progression. UGDH expression is high in the normal prostate even though hyaluronan accumulation is virtually undetectable. The enzyme's common role in the prostate may be to provide precursors for glucuronosyltransferase enzymes, which inactivate and solubilize androgens by glucuronidation. Androgen dependence of UGDH, glucuronosyltransferase, and hyaluronan synthase expression, overview
physiological function
enzyme displays hysteresis, observed as a lag in progress curves, and is sensitive to product inhibition during the lag. The inhibition results in a systematic decrease in steady-state velocity and makes the lag appear to have a second-order dependence on enzyme concentration.The lag is in fact due to a substrate and cofactor-induced isomerization of the enzyme. The cofactor binds to the enzyme:substrate complex with negative cooperativity, suggesting that the isomerization may be related to the formation of an asymmetric enzyme complex. The hysteresis may be the consequence of a functional adaptation, by slowing the response of the enzyme to sudden increases in the flux of substrate, the other biochemical pathways that use this important metabolite will have a competitive edge
physiological function
precise allelic exchange mutagenesis of isoform hasB in strain 5448, a representative of the globally disseminated M1T1 serotype, does not abolish hyaluronic acid capsule synthesis due to presence of paralog HasB2. Mutagenesis of HasB2 alone slightly decreases capsule abundance. A HasB HasB2 double mutant becomes completely acapsular
physiological function
precise allelic exchange mutagenesis of isoform hasB in strain 5448, a representative of the globally disseminated M1T1 serotype, does not abolish hyaluronic acid capsule synthesis due to presence of paralog HasB2. Mutagenesis of HasB2 alone slightly decreases capsule abundance. A HasB HasB2 double mutant becomes completely acapsular
physiological function
the enzyme is involved in protein N-glycosylation
physiological function
enzyme AglM can be functionally replaced by another UDP-glucose dehydrogenase, VNG1048G, in vivo
physiological function
enzyme VNG1048G can functionally replace another UDP-glucose dehydrogenase AglM in vivo. In Halobacterium salinarum, where glycoproteins are modified by an N-linked glycan of similar composition, gene VNG1048G is not only found within a cluster of N-glycosylation-related genes reminiscent of the genomic region surrounding its Haloferax volcanii counterpart AglM but can also functionally replace gene aglM in a Haloferax volcanii strain lacking the gene
physiological function
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in Escherichia coli K-12, Ugd is important for biosynthesis of the environmentally regulated exopolysaccharide known as colanic acid, whereas in other Escherichia coli isolates, the same enzyme is required for production of the constitutive group 1 capsular polysaccharides, which act as virulence determinants
physiological function
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in Escherichia coli serotype K30, the enzyme is required for production of the constitutive group 1 capsular polysaccharides, which act as virulence determinants
physiological function
the enzme synthesize UDP-glucuronate, a key sugar nucleotide involved in biosynthesis of the plant cell wall, the LgUGDH gene plays a role in controlling the biosynthesis of secondary cell walls
physiological function
the enzyme is involved in the biosnthesis of the Ss sphingan biopolymer
physiological function
the enzyme provides UDP-glucuronic acid for the synthesis of the exopolysaccharide gellan
physiological function
UDP-glucose dehydrogenase activity and optimal downstream cellular function require dynamic reorganization at the dimer-dimer subunit interfaces
physiological function
UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview
physiological function
UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview. UDP-glucuronic acid is a key precursor for the synthesis of the glycosaminoglycan chain in proteoglycans
physiological function
enzyme is involved in capsular polysaccharide biosynthesis
physiological function
epirubicin accumulation increases and apoptosis decreases during UGDH knockdown. Hyaluronan-coated matrix increases and a positive modulation of autophagy is detected. Higher levels of UGDH are correlated with worse prognosis in triple-negative breast cancer patients that receive chemotherapy. High expression of UGDH is found in tumoral tissue from HER2--patients. UGDH knockdown contributes to epirubicin resistance
physiological function
in breast cancer cells, depletion of the hyaluronic acid precursor UDP-glucuronic acid is sufficient to inhibit several mesenchymal-like properties including cellular invasion and colony formation in vitro, as well as tumor growth and metastasis in vivo. Depletion of UDP-glucuronic acid alters the expression of PPAR-gamma target genes and increases PPAR-gamma DNA binding activity
physiological function
knocking out UGDH in highly metastatic 6DT-1 breast cancer cells impairs migration ability without affecting in vitro proliferation. UGDH-KO results in significantly decreased metastatic capacity in vivo when the cells are orthotopically injected in syngeneic mice
physiological function
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the ectopic overexpression of UGDH4 in Arabidopsis thaliana significantly increases the contents of hemicellulose and soluble sugar
physiological function
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transgenic Arabidopsis lines overexpressing GH_D12G1806 have longer root lengths and higher gene expression level than the wild-type plants of Columbia-0. At flowering stage, the number of trichomes on the sepals of transgenic lines increases significantly, to about 155% of that of the control plants. Compared with the Col-0, most of the trichomes on the main stem of transgenic lines show bifurcated phenotypes
physiological function
UDP-glucose dehydrogenase Ugd2 is involved in building capsular polysaccharides K20 and K21. The K20 and K21 capsular polysaccharides include GlcpA produced by Ugd2 and D-galactose with an (R)-configured 4,6-pyruvic acid acetal added by Prt2. The first sugar in the tetrasaccharide K units is 2-acetamido-4-amino-2,4,6-trideoxy-D-glucose (D-QuipNAc4N) that carries a 4-N-[(S)-3-hydroxybutanoyl] group in some K units and a 4-N-acetyl group in the others
physiological function
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precise allelic exchange mutagenesis of isoform hasB in strain 5448, a representative of the globally disseminated M1T1 serotype, does not abolish hyaluronic acid capsule synthesis due to presence of paralog HasB2. Mutagenesis of HasB2 alone slightly decreases capsule abundance. A HasB HasB2 double mutant becomes completely acapsular
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physiological function
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enzyme is involved in capsular polysaccharide biosynthesis
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physiological function
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UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview
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physiological function
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precise allelic exchange mutagenesis of isoform hasB in strain 5448, a representative of the globally disseminated M1T1 serotype, does not abolish hyaluronic acid capsule synthesis due to presence of paralog HasB2. Mutagenesis of HasB2 alone slightly decreases capsule abundance. A HasB HasB2 double mutant becomes completely acapsular
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physiological function
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the enzyme is involved in the biosnthesis of the Ss sphingan biopolymer
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physiological function
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the enzyme provides UDP-glucuronic acid for the synthesis of the exopolysaccharide gellan
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physiological function
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UDP-glucose dehydrogenase is responsible for the NAD-dependent twofold oxidation of UDP-glucose to UDP-glucuronic acid, one of the key components for gellan biosynthesis
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physiological function
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the enzyme is involved in protein N-glycosylation
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physiological function
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enzyme AglM can be functionally replaced by another UDP-glucose dehydrogenase, VNG1048G, in vivo
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physiological function
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enzyme VNG1048G can functionally replace another UDP-glucose dehydrogenase AglM in vivo. In Halobacterium salinarum, where glycoproteins are modified by an N-linked glycan of similar composition, gene VNG1048G is not only found within a cluster of N-glycosylation-related genes reminiscent of the genomic region surrounding its Haloferax volcanii counterpart AglM but can also functionally replace gene aglM in a Haloferax volcanii strain lacking the gene
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additional information
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dysregulated expression of UGDH can promote the development of androgen independent tumor cell growth by increasing available levels of intracellular androgen. UGDH activity is the rate limiting factor in solubilization of excess androgen from prostate tumor cells, overview
additional information
mutation in either ugd leads to activation of RpoE, an extracytoplasmic function sigma factor that is activated by protein misfolding and alterations in cell surface structure in other bacteria. Activation of RpoE or RpoE overexpression causes inhibition of FlhDC and hemolysin expression
additional information
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mutation in either ugd leads to activation of RpoE, an extracytoplasmic function sigma factor that is activated by protein misfolding and alterations in cell surface structure in other bacteria. Activation of RpoE or RpoE overexpression causes inhibition of FlhDC and hemolysin expression
additional information
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enzyme Ugd from Escherichia coli K-12 can functionally replace enzyme Ugd from Escherichia coli serotype K30 in biosynthesis of K30 capsular polysaccharide
additional information
Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
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Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
surface-exposed residues in homology models of the UDP-glucose dehydrogenase reveals the more acidic and less basic VNG1048G surface, explaining the salt-dependence of the Halobacterium salinarum enzyme. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
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surface-exposed residues in homology models of the UDP-glucose dehydrogenase reveals the more acidic and less basic VNG1048G surface, explaining the salt-dependence of the Halobacterium salinarum enzyme. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
the active site of UgdG bound to UDP-Glc and coenzyme NADH contains 6 highly conserved residues: Thr122, Glu151, Lys207, Asn211, Cys263 and Asp267. Residue Cys263 is a clear candidate for the catalytic nucleophile of the reaction. Tyr10 plays a catalytic role in the final hydrolysis of UDP-Glc
additional information
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the active site of UgdG bound to UDP-Glc and coenzyme NADH contains 6 highly conserved residues: Thr122, Glu151, Lys207, Asn211, Cys263 and Asp267. Residue Cys263 is a clear candidate for the catalytic nucleophile of the reaction. Tyr10 plays a catalytic role in the final hydrolysis of UDP-Glc
additional information
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the active site of UgdG bound to UDP-Glc and coenzyme NADH contains 6 highly conserved residues: Thr122, Glu151, Lys207, Asn211, Cys263 and Asp267. Residue Cys263 is a clear candidate for the catalytic nucleophile of the reaction. Tyr10 plays a catalytic role in the final hydrolysis of UDP-Glc
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additional information
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Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
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additional information
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surface-exposed residues in homology models of the UDP-glucose dehydrogenase reveals the more acidic and less basic VNG1048G surface, explaining the salt-dependence of the Halobacterium salinarum enzyme. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
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Y10F
mutation in GXGYXG consensus motif, 9% residual activity. Tyr10 plays a catalytic role in the final hydrolysis step. Upon release of NADH after the second oxidation step, Tyr10 may work as a proton conveyer from the aqueous hydrogen-bonding proton wire system to the hydrolytic site
Y10K
mutation in GXGYXG consensus motif, 2% residual activity
Y10S
mutation in GXGYXG consensus motif, 3% residual activity
I331D
hypomorphic loss-of-function mutation jekyll m151. contrary to humans, homozygous mutant larvae do not show signs of increased c-fos expression at basal state
K323A
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R324A
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site-directed mutagenesis, the mutant purifies in much lower amounts relative to wild-type and is prone to degradation and has negligible activity
Y71F
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site-directed mutagenesis, the mutant shows unaltered catalytic activity
A104L
ubstitution introduced to fill a cavity in the E state and sterically prevent repacking of the core into the inactive Eomega state. Mutant A104L does not show hysteresis or negative cooperativity, binds UDP-xylose with lower affinity and the inhibition is no longer cooperative
A136M
mutant does not exhibit substrate cooperativity. The inhibitor affinity of A136M is reduced 14fold and does not exhibit hysteresis. Substitution disrupts NAD+-induced negative cooperativity
A44V
mutation is the genetic cause of a developmental epileptic encephalopathy in a consanguineous Palestinian family with three affected siblings. The A44V variant is also found in two additional families from Puerto Rico and from Spain
C276E
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activity is not measurable at pH 8.7, 22°C
C276G
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activity is not measurable at pH 8.7, 22°C
C276K
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activity is not measurable at pH 8.7, 22°C
C276L
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activity is not measurable at pH 8.7, 22°C
C276Y
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activity is not measurable at pH 8.7, 22°C
D280A
extremely poor enzymic activity
D280E
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site-directed mutagenesis, 3-fold increase in Km for UDP-glucose and a 2-fold reduced Vmax relative to that of the wild type
DELTA132
deletion of residue Val132 from the Thr131 loop to approximate an intermediate state in the allosteric transition. The crystal structure of the deletion construct reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the construct as a hexamer with point group symmetry 32, similar to that of the active complex. The DELTA132 and UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces
E110A
site-directed mutagenesis, the mutant, although dimeric in the apo form, exhibits only about 50% reduction in Vmax, but is highly unstable in solution and in cultured cells so it cannot be evaluated unambiguously
E161Q
hydrolysis step becomes completely rate-limiting so that a thioester enzyme intermediate accumulates at steady state. Crystallization of E161Q in the presence of 5 mM UDP-glucose and 2 mM NAD results in trapping a thiohemiacetal enzyme intermediate
G13E
normal expression and stability of mutant, no enzymic activity, no photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
K220H
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site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K220R
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site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
N224A
steady-state kinetic parameters are within an order of magnitude of the native enzyme
T131S
steady-state kinetic parameters are within an order of magnitude of the native enzyme
T325A
site-directed mutagenesis, the mutant occurs as dimeric species that can be induced to form hexamers in the ternary complex with substrate and cofactor. The inducible hexamer shows that upon increasing enzyme concentration, which favors the hexameric species, activity is modestly decreased and exhibits cooperativity. The T325A mutant is significantly less efficient in promoting downstream hyaluronan production by HEK293 cells than the wild-type. The activity of the T325A mutant is the most labile, with a half-life of only 24 h that is not extended significantly by substrate and cofactor addition
T325D
site-directed mutagenesis, the mutant yields exclusively dimeric species. The T325D mutant is significantly less efficient in promoting downstream hyaluronan production by HEK293 cells than the wild-type. UGDH T325D retains its activity similarly to the wild-type enzyme but does not exhibit increased stability in the abortive ternary complex
E141Q
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kcat-value 10fold lower than wild-type
E145Q
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kcat-value 10fold lower than wild-type
T118A
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160fold reduction of kcat value
A222Q/S233G
-
mutation does not affect expression, stability, and secondary structure. Mutant protein is a dimer and catalytic active, with increased Km values for substrates
A222Q/S233G
is a dimer in solution
C276A
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site-directed mutagenesis, strong decrease in specific activity
C276A
is a hexamer-dimer mixture
C276S
no enzymic activity, affinity for NAD+ similar to wild-type, retains predominantly hexameric structure
C276S
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site-directed mutagenesis, strong decrease in specific activity
D280N
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site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
D280N
shows, exclusively, a hexameric quaternary structure in solution
D280N
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an inactive UGDH mutant
K220A
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site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K220A
shows, exclusively, a hexameric quaternary structure in solution
K220A
extremely poor enzymic activity
K279A
no enzymic activity, affinity for NAD+ similar to wild-type, almost exclusively found as dimer
K279A
-
site-directed mutagenesis, strong decrease in specific activity
K279A
is essentially a dimer
K339A
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site-directed mutagenesis, 165fold decrease in affinity for UDP-glucose. Mutant forms a dimer, in contrast to hexameric wild-type
K94E
mutation in the hexamer-building interface, generates a stable enzyme dimer. 160fold decrease in kcat value
K94E
substitution prevents hexamer formation. Mutant does not display hysteresis
C260A
-
mutation of the essential Cys residue. The C260A mutant and wild-type are then co-expressed in vivo via a single-crossover homologous recombination method. The resulting strain produces an amide derivative of hyaluronan
C260A
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no oxidation of UDP-glucose to glucuronic acid, but capable of both reducing the aldehyde intermediate and oxidizing the hydrated form of the aldehyde intermediate, protein is expressed in inclusion bodies
additional information
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differences in host colonization between wild-type and UDPDH mutant
additional information
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comparison of sequence homologies with bacterial enzymes
additional information
inactivation of gene Ugd(BCAL2946) results in increased sensitivity to polymyxin B and this sensitivity can be overcome when either genes Ugd(BCAL2946) or Ugd(BCAM0855) but not gene ugd(BCAM2034) is expressed from plasmids. Growth of a conditional Ugd(BCAL2946) mutant, created in the DELTAUgd(BCAM0855) background, is significantly impaired under non-permissive conditions. Growth can be rescued by either Ugd(BCAL2946) or Ugd(BCAM0855) expressed in trans, but not by Ugd(BCAM2034)
additional information
inactivation of gene Ugd(BCAL2946) results in increased sensitivity to polymyxin B and this sensitivity can be overcome when either genes Ugd(BCAL2946) or Ugd(BCAM0855) but not gene ugd(BCAM2034) is expressed from plasmids. Growth of a conditional Ugd(BCAL2946) mutant, created in the DELTAUgd(BCAM0855) background, is significantly impaired under non-permissive conditions. Growth can be rescued by either Ugd(BCAL2946) or Ugd(BCAM0855) expressed in trans, but not by Ugd(BCAM2034)
additional information
inactivation of gene Ugd(BCAL2946) results in increased sensitivity to polymyxin B and this sensitivity can be overcome when either genes Ugd(BCAL2946) or Ugd(BCAM0855) but not gene ugd(BCAM2034) is expressed from plasmids. Growth of a conditional Ugd(BCAL2946) mutant, created in the DELTAUgd(BCAM0855) background, is significantly impaired under non-permissive conditions. Growth can be rescued by either Ugd(BCAL2946) or Ugd(BCAM0855) expressed in trans, but not by Ugd(BCAM2034)
additional information
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overexpression of enzyme plus transformation of gene cluster for K5 polysaccharide production, 15fold increase in enzyme activity, decrease in K5 polysaccharide formation
additional information
-
enzyme Ugd from Escherichia coli K-12 can functionally replace enzyme Ugd from Escherichia coli serotype K30 in biosynthesis of K30 capsular polysaccharide
additional information
perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the hUGDH structure, thereby changing the motional fluctuation pattern at the oligomeric interfaces. A large-magnitude cooperative motion at the oligomeric interfaces is a critical factor in interfering with the hexamer formation of the enzyme. Structural stability at the dimeric interface is necessary to retain the hexameric structure of UGDH
additional information
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perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the hUGDH structure, thereby changing the motional fluctuation pattern at the oligomeric interfaces. A large-magnitude cooperative motion at the oligomeric interfaces is a critical factor in interfering with the hexamer formation of the enzyme. Structural stability at the dimeric interface is necessary to retain the hexameric structure of UGDH
additional information
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UGDH overexpression stimulates hyaluronan production in HEK293 cells
additional information
UDP-glucose dehydrogenase mutants are engineered to perturb hexamer:dimer quaternary structure equilibrium. Dimeric species of UGDH have reduced activity in vitro and in supporting hyaluronan production by cultured cells. The purified enzymes reveal a significant decrease in the enzymatic activity of the obligate dimer and hexamer mutants. The activity of the truncated DELTA132 mutant is negligible. The half-life of UGDH catalytic activity in vitro is reduced by mutations at the dimer interface
additional information
UGDH specific siRNAs markedly inhibits UGDH mRNA and protein expression, and leads to an obvious suppression of PGs synthesis in human articular chondrocytes
additional information
introduction of site-specific unnatural amino acids to facilitate crosslinking of monomeric subunits into predominantly obligate oligomeric species. Optimal crosslinking is achieved by encoding 4-benzoyl-L-phenylalanine at position 458, and exposing to long wavelength UV in the presence of substrate and cofactor. Purified hexameric complexes contain significant fractions of dimer and trimer (approximately 50%) along with another 10% tetramer and higher molecular mass species. Activity of the crosslinked enzyme is reduced by almost 60% relative to the uncrosslinked UGDH mutant
additional information
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introduction of site-specific unnatural amino acids to facilitate crosslinking of monomeric subunits into predominantly obligate oligomeric species. Optimal crosslinking is achieved by encoding 4-benzoyl-L-phenylalanine at position 458, and exposing to long wavelength UV in the presence of substrate and cofactor. Purified hexameric complexes contain significant fractions of dimer and trimer (approximately 50%) along with another 10% tetramer and higher molecular mass species. Activity of the crosslinked enzyme is reduced by almost 60% relative to the uncrosslinked UGDH mutant
additional information
construction by Tn5 transposon mutagenesis of a knockout mutant of ugd, that is extremely sensitive to polymyxin B, presumably because of alterations in lipopolysaccharide structure and cell surface architecture in the mutant. The mutant is defective in swarming, expresses lower levels of virulence factor hemolysin, and has lower cell invasion ability. Complementation of the ugd or galU mutant with the full-length ugd gene leads to the restoration of wild-type phenotypic traits, phenotype, overview
additional information
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construction by Tn5 transposon mutagenesis of a knockout mutant of ugd, that is extremely sensitive to polymyxin B, presumably because of alterations in lipopolysaccharide structure and cell surface architecture in the mutant. The mutant is defective in swarming, expresses lower levels of virulence factor hemolysin, and has lower cell invasion ability. Complementation of the ugd or galU mutant with the full-length ugd gene leads to the restoration of wild-type phenotypic traits, phenotype, overview
additional information
mutant lacking PA2022 activity and double mutant lacking PA2022 and isoform PA3559 activity are more susceptible to chloramphenicol, ceffotaxime, and ampicillin
additional information
mutant lacking PA2022 activity and double mutant lacking PA2022 and isoform PA3559 activity are more susceptible to chloramphenicol, ceffotaxime, and ampicillin
additional information
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mutant lacking PA2022 activity and double mutant lacking PA2022 and isoform PA3559 activity are more susceptible to chloramphenicol, ceffotaxime, and ampicillin
additional information
mutant lacking PA3559 activity shows reduced resistance to polymyxin B
additional information
mutant lacking PA3559 activity shows reduced resistance to polymyxin B
additional information
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mutant lacking PA3559 activity shows reduced resistance to polymyxin B
additional information
overexpression of the ugdG gene in Sphingomonas sanxanigenens results in increased sphingan Ss production and higher fermentation broth viscosity. The weightaverage molecular weight of polymer Ss from the recombinant strain is higher and the viscosity is higher than those from the wild-type strain at a shear rate of 1 rev/min
additional information
-
overexpression of the ugdG gene in Sphingomonas sanxanigenens results in increased sphingan Ss production and higher fermentation broth viscosity. The weightaverage molecular weight of polymer Ss from the recombinant strain is higher and the viscosity is higher than those from the wild-type strain at a shear rate of 1 rev/min
additional information
-
overexpression of the ugdG gene in Sphingomonas sanxanigenens results in increased sphingan Ss production and higher fermentation broth viscosity. The weightaverage molecular weight of polymer Ss from the recombinant strain is higher and the viscosity is higher than those from the wild-type strain at a shear rate of 1 rev/min
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Haloferax volcanii (D4GYH5), Haloferax volcanii, Halobacterium salinarum (Q9HQQ9), Halobacterium salinarum, Haloferax volcanii ATCC 29605 (D4GYH5), Halobacterium salinarum ATCC 700922 (Q9HQQ9)
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Caenorhabditis elegans (Q19905), Caenorhabditis elegans
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Inhibiting hexamer disassembly of human UDP-glucose dehydrogenase by photoactivated amino acid cross-linking
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Homo sapiens (O60701), Homo sapiens
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Beattie, N.; Keul, N.; Sidlo, A.; Wood, Z.
Allostery and hysteresis are coupled in human UDP-glucose dehydrogenase
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Homo sapiens (O60701), Homo sapiens
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Beattie, N.R.; Pioso, B.J.; Sidlo, A.M.; Keul, N.D.; Wood, Z.A.
Hysteresis and allostery in human UDP-glucose dehydrogenase require a flexible protein core
Biochemistry
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Homo sapiens (O60701), Homo sapiens
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Riegert, A.; Raushel, F.
Functional and structural characterization of the UDP-glucose dehydrogenase involved in capsular polysaccharide biosynthesis from Campylobacter jejuni
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2021
Campylobacter jejuni subsp. jejuni (Q0P8H3), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q0P8H3)
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Initial identification of UDP-glucose dehydrogenase as a prognostic marker in breast cancer patients, which facilitates epirubicin resistance and regulates hyaluronan synthesis in MDA-MB-231 cells
Biomolecules
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2021
Homo sapiens (O60701), Homo sapiens
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Homo sapiens (O60701), Homo sapiens
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Homo sapiens (O60701), Mus musculus (O70475), Mus musculus
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UDP-glucose dehydrogenases identification, expression, and function analyses in upland cotton (Gossypium hirsutum)
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Acinetobacter baumannii K20 and K21 capsular polysaccharide structures establish roles for UDP-glucose dehydrogenase Ugd2, pyruvyl transferase Ptr2 and two glycosyltransferases
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Acinetobacter baumannii (A0A2H4ZRD7), Acinetobacter baumannii
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Streptococcus equi subsp. zooepidemicus
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Targeting UDP-glucose dehydrogenase inhibits ovarian cancer growth and metastasis
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Homo sapiens (O60701), Homo sapiens
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Homo sapiens (O60701), Homo sapiens
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Hengel, H.; Bosso-Lefevre, C.; Grady, G.; Szenker-Ravi, E.; Li, H.; Pierce, S.; Lebigot, E.; Tan, T.T.; Eio, M.Y.; Narayanan, G.; Utami, K.H.; Yau, M.; Handal, N.; Deigendesch, W.; Keimer, R.; Marzouqa, H.M.; Gunay-Aygun, M.; Muriello, M.J.; Verhelst, H.; Weckhuysen, S.; Mahida, S.; Naidu, S.; Thomas, T.G.
Loss-of-function mutations in UDP-glucose 6-dehydrogenase cause recessive developmental epileptic encephalopathy
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Danio rerio (A8WGP7), Danio rerio, Homo sapiens (O60701), Homo sapiens
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UDP-glucose 6-dehydrogenase regulates hyaluronic acid production and promotes breast cancer progression
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2020
Homo sapiens (O60701), Homo sapiens
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Wei, S.; Zhang, X.Y.; Sun, Y.; Conway, L.P.; Liu, L.
Discovery and biochemical characterization of UDP-Glucose dehydrogenase from Akkermansia muciniphila
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Akkermansia muciniphila
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Yang, Y.; Kang, L.; Wu, R.; Chen, Y.; Lu, C.
Genome-wide identification and characterization of UDP-glucose dehydrogenase family genes in moso bamboo and functional analysis of PeUGDH4 in hemicellulose synthesis
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Phyllostachys edulis
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