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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-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+
-
-
-
-
?
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-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+
-
-
-
?
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 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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
no reaction with NADP+
-
-
-
additional information
?
-
-
no reaction with ethylnicotinate adenine dinucleotide
-
-
-
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
no reaction with alpha-NAD+
-
-
-
additional information
?
-
-
no reaction with 3-formylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
thionicotinamide adenine dinucleotide
-
-
-
additional information
?
-
-
no reaction with deamino-NAD+
-
-
-
additional information
?
-
-
no reaction with 3-propionylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
nicotinamide hypoxanthine dinucleotide
-
-
-
additional information
?
-
-
no reaction with alpha-NAD+
-
-
-
additional information
?
-
Saccharum spp.
-
no substrate: ADP-glucose
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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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UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
additional information
?
-
-
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
-
-
-
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+
-
-
-
?
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+
-
-
-
-
?
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-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-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+
-
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+
-
-
-
?
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
-
-
?
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0.05617
5-azido-UDP-glucose
-
22°C, pH 8.7
0.058
aldehyde intermediate
-
-
-
0.015 - 2.21
UDP-alpha-D-glucose
additional information
additional information
-
0.006
NAD+

-
37°C, pH 10.5
0.042
NAD+
-
isoform Ugd3, pH 8.7, 22°C
0.043
NAD+
-
isoform Ugd2, pH 8.7, 22°C
0.044
NAD+
-
isoform Ugd4, pH 8.7, 22°C
0.0722
NAD+
Saccharum spp.
-
pH 8.4, 25°C
0.1
NAD+
-
mutant E161Q, pH 8.7, 25°C
0.132
NAD+
-
pH 8.8, 25°C
0.133
NAD+
-
wild-type, pH 8.7, 22°C
0.135
NAD+
-
mutant E141Q
0.16
NAD+
-
50°C, pH 10.5
0.187
NAD+
-
mutant E145Q
0.31
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme
0.35 - 0.62
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme, from different strains; pH 9.5, 37°C, recombinant wild-type enzyme, with 0.025-1.0 mM ATP
0.38
NAD+
pH 8.7, 37°C, recombinant enzyme
0.384
NAD+
-
wild-type, pH 8.7, 25°C
0.401
NAD+
-
mutant A222Q/S233G, pH 8.7, 22°C
0.42
NAD+
-
wild-type, pH 7.4, 22°C
0.43
NAD+
-
pH 9.5, 37°C, recombinant mutant K323A
0.5
NAD+
-
pH 9.5, 37°C, recombinant mutant Y71F
0.53
NAD+
-
mutant K339A, pH 7.4, 22°C
0.53
NAD+
wild-type, pH 8.7, 30°C, Hill-coefficient 1.5
0.646
NAD+
-
pH 7.4, 37°C, recombinant His-tagged wild-type enzyme
0.69
NAD+
-
70°C, pH 10.5
0.7
NAD+
-
wild-type, pH 8.7, 25°C
0.897
NAD+
-
pH 7.4, 37°C, recombinant His-tagged mutant T325A
0.942
NAD+
-
wild-type, pH 7.5, 25°C, Hill coefficient 0.74
1.084
NAD+
-
pH 7.4, 37°C, recombinant His-tagged mutant T325D
2.1
NAD+
-
mutant K339A, pH 7.4, 22°C
2.92
NAD+
-
mutant K94E, pH 7.5, 25°C
6.3
NAD+
-
mutant K94E, pH 8.7, 25°C
0.017
UDP

-
wild-type, pH 8.7, 22°C
0.98
UDP
-
mutant A222Q/S233G, pH 8.7, 22°C
0.015
UDP-alpha-D-glucose

-
pH 7.4, 37°C, recombinant His-tagged mutant T325D
0.016
UDP-alpha-D-glucose
-
wild-type, pH 7.5, 25°C
0.021
UDP-alpha-D-glucose
-
pH 8.8, 25°C
0.025
UDP-alpha-D-glucose
-
wild-type, pH 8.7, 25°C
0.034
UDP-alpha-D-glucose
-
pH 7.4, 37°C, recombinant His-tagged wild-type enzyme
0.035
UDP-alpha-D-glucose
-
wild-type, pH 8.7, 25°C
0.048
UDP-alpha-D-glucose
-
pH 7.4, 37°C, recombinant His-tagged mutant T325A
0.055
UDP-alpha-D-glucose
-
mutant E161Q, pH 8.7, 25°C
0.0958
UDP-alpha-D-glucose
pH 8.4, 30°C
0.23
UDP-alpha-D-glucose
wild-type, pH 8.7, 30°C, Hill-coefficient 0.89
0.269
UDP-alpha-D-glucose
-
mutant K94E, pH 7.5, 25°C
0.32
UDP-alpha-D-glucose
-
37°C, pH 10.5
0.42
UDP-alpha-D-glucose
-
50°C, pH 10.5
0.47
UDP-alpha-D-glucose
pH 8.7, 37°C, recombinant enzyme
1.28
UDP-alpha-D-glucose
-
70°C, pH 10.5
2.21
UDP-alpha-D-glucose
-
mutant K94E, pH 8.7, 25°C
0.0092
UDP-glucose

-
wild-type, pH 7.4, 22°C
0.011
UDP-glucose
pH 7.4, 22°C
0.017
UDP-glucose
pH 8.7, 25°C
0.01703
UDP-glucose
-
22°C, pH 8.7
0.0187
UDP-glucose
Saccharum spp.
-
pH 8.4, 25°C
0.02
UDP-glucose
-
wild-type
0.022
UDP-glucose
-
pH 8.7, 25°C
0.022
UDP-glucose
-
mutant K339A, pH 7.4, 22°C
0.059
UDP-glucose
-
mutant T118A
0.06
UDP-glucose
-
mutant E141Q
0.12
UDP-glucose
pH 7.5, 22°C
0.123
UDP-glucose
-
isoform Ugd2, pH 8.7, 22°C
0.125
UDP-glucose
-
mutant E145Q
0.171
UDP-glucose
-
isoform Ugd4, pH 8.7, 22°C
0.2
UDP-glucose
pH 8.7, 22°C
0.335
UDP-glucose
-
isoform Ugd3, pH 8.7, 22°C
0.38
UDP-glucose
-
20°C, pH 8, UDPGDH-A
0.4
UDP-glucose
pH 7.5, 22°C
0.87
UDP-glucose
-
pH 8.7, 30°C
0.95
UDP-glucose
-
20°C, pH 8, UDPGDH-B
1.5
UDP-glucose
-
mutant K339A, pH 7.4, 22°C
0.015
UDPglucose

-
pH 9.4
0.035
UDPglucose
-
pH 8.6
0.0756
UDPglucose
-
native enzyme
1
UDPglucose
-
dissociated enzyme
8.4
UDPglucose
-
recombinant glutathione-S-transferase fusion protein
additional information
additional information

-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
pH-dependence of Km
-
additional information
additional information
-
KM increase at pH higher than 9.0
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetic, cooperative kinetic behavior occurs in the hexameric enzyme
-
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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
-
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
-
the enzyme belongs to the the UGDH family of proteins
-
malfunction

-
Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
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
UGDH protein level in rat osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis
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
-
Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
-
malfunction
-
UGDH protein level in rat osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis
-
metabolism

the enzyme participates in sucrose/polysaccharide metabolism and cell wall biosynthesis
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
-
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
-
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
-
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
the enzyme is involved in the biosnthesis of the Ss sphingan biopolymer
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
UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview
physiological function
the enzyme provides UDP-glucuronic acid for the synthesis of the exopolysaccharide gellan
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
-
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; 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
-
UDP-glucose dehydrogenase activity and optimal downstream cellular function require dynamic reorganization at the dimer-dimer subunit interfaces
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
-
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
-
enzyme AglM can be functionally replaced by another UDP-glucose dehydrogenase, VNG1048G, in vivo
-
physiological function
-
the enzyme is involved in protein N-glycosylation
-
physiological function
-
UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview
-
physiological function
-
the enzyme provides UDP-glucuronic acid for the synthesis of the exopolysaccharide gellan; 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
-
the enzyme is involved in the biosnthesis of the Ss sphingan biopolymer
-
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
-
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
-
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
-
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
-
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
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
-
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
-
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
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
-
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
-
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
-
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dimer or hexamer
-
x * 57000, recombinant enzyme, SDS-PAGE
homodimer
recombinant form of Ugd(BCAL2946); recombinant form of Ugd(BCAM0855)
?

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x * 52600, recombinant His6-tagged BceC, SDS-PAGE
?
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x * 52600, recombinant His6-tagged BceC, SDS-PAGE
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?
x * 56300, calculated, x * 60000, SDS-PAGE
?
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x * 56300, calculated, x * 60000, SDS-PAGE
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?
x * 53100, deduced from gene sequence
?
Saccharum spp.
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x * 52000, SDS-PAGE
?
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x * 48500, SDS-PAGE and calculated for His-tagged protein
?
x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE
?
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x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE
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?
x * 48200, about, sequence calculation
?
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x * 48200, about, sequence calculation
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?
x * 42000, SDS-PAGE, x * 43400, calculated
?
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x * 42000, SDS-PAGE, x * 43400, calculated
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dimer

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2 * 47000, SDS-PAGE
dimer
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2 * 44000, SDS-PAGE
dimer
2 * 47000, about, SDS-PAGE
dimer
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2 * 47000, about, SDS-PAGE
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dimer
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2 * 57000, mutant A222Q/S233G and part of wild-type, SDS-PAGE
dimer
54500, calculated; 57400, calculated
dodecamer

12 * 47000, about, SDS-PAGE
dodecamer
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12 * 47000, about, SDS-PAGE
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dodecamer
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12 * 47000, about, SDS-PAGE
dodecamer
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12 * 47000, about, SDS-PAGE
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hexamer

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6 * 52000, at pH 5.5-7.8, equilibrium measurement under native and denaturing conditions
hexamer
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6 * 52000, gel filtration
hexamer
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6 * 50000, SDS-PAGE
hexamer
6 x 57000, SDS-PAGE
hexamer
6 * 57000, SDS-PAGE
hexamer
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6* 57000, wild-type, plus some dimer and monomer, SDS-PAGE
monomer

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1 * 55000, SDS-PAGE
monomer
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1 * 57000, SDS-PAGE, minor part of wild-type, major part is hexamer
monomer
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1 * 50000, SDS-PAGE
monomer
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1 * 45500, SDS-PAGE
tetramer

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-
tetramer
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4 * 70000, gel filtration after treatment with SDS
additional information

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structural modelling of the enzyme in complex with NAD and uridine 5'-monophosphate, using structure of Ugd from Klebsiella pneumoniae in complex with UDPGA, PDB ID 3PJG, as template
additional information
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the specific activity of the VNG1048G dodecamer at 2 M NaCl is only one sixth of that of UDP-glucose dehydrogenase AglM, while the dimer is inactive. The oligomeric status of VNG1048G is affected by lowered salinity. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
the specific activity of the VNG1048G dodecamer at 2 M NaCl is only one sixth of that of UDP-glucose dehydrogenase AglM, while the dimer is inactive. The oligomeric status of VNG1048G is affected by lowered salinity. 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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the specific activity of the VNG1048G dodecamer at 2 M NaCl is only one sixth of that of UDP-glucose dehydrogenase AglM, while the dimer is inactive. The oligomeric status of VNG1048G is affected by lowered salinity. 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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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
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additional information
significant amount of dimeric and monomeric species can be detected
additional information
identification of amino acids I7 through T19 as NAD+ binding-site by photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
additional information
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examination of the dimer-dimer subunit interface reveals an extensive network of charge interactions and hydrogen bonding that coordinately stabilize the hexamer in the presence and absence of its cofactor or substrate, involving residue T325. The wild-type UGDH enzyme purifies in a hexamer-dimer equilibrium and transiently undergoes dynamic motion that exposes the dimer-dimer interface during catalysis. Only dynamic UGDH hexamers support robust cellular function, mutant dimeric species of UGDH have reduced activity in vitro and in supporting hyaluronan production by cultured cells. Molecular interactions at the subunit interface, overview. In the apo form Thr325 directly forms a hydrogen bond with Asp105 of the opposite subunit
additional information
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
additional information
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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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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
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
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
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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
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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
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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
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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
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steady-state kinetic parameters are within an order of magnitude of the native enzyme
T131S
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steady-state kinetic parameters are within an order of magnitude of the native enzyme
T325A
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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
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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
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
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

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