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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
-
-
?
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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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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?