HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.1.1.22 - UDP-glucose 6-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.22Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.22 UDP-glucose 6-dehydrogenaseIUBMB Comments
Also acts on UDP-alpha-D-2-deoxyglucose.
Specify your search results
Word Map
- 1.1.1.22
-
udp-glucuronic
- polysaccharide
- glycosaminoglycans
- hyaluronan
- udp-xylose
-
pyrophosphorylase
-
glucuronidation
-
glucuronic
- exopolysaccharide
- udp-glca
- udp-sugars
-
udp-glucuronyltransferase
-
glca
-
udpga
- udp-d-glucuronate
- agriculture
- pharmacology
- synthesis
- molecular biology
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
udp-glucose dehydrogenase, udpgdh, udpgd, uridine diphosphoglucose dehydrogenase, udp-glucose 6-dehydrogenase, udpglucose dehydrogenase, udp-gdh, udp-glc dehydrogenase, udpg dehydrogenase, udp-glcdh, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AglM
BceC
HasB
HasB2
HVO_1531
UDG1
UDP-GlcDH
UDP-GlcDHase
UDP-glucose dehydrogenase
UDPGDH
UDPglucose dehydrogenase
Ugd
UgdG
UGDH
uridine-5'-diphosphoglucose dehydrogenase
VNG1048G
VNG_1048G
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
reaction mechanism, C275 provides SH-group in the catalytic centre
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
two-step reaction, reaction mechanism
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
ping-pong reaction mechanism
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
also shows aldehyde dehydrogenase activity
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
also shows alcohol dehydrogenase activity
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
also shows alcohol dehydrogenase activity
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
bi-uni-uni-bi mechanism
Saccharum spp.
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
mechanism, ordered water molecule H-bonded to T118 serves as catalytic base in hydride transfer
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
the enzyme is also binds RNA and acts as a ribonuclease
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
the enzyme is also binds RNA and acts as a ribonuclease
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:NAD+ 6-oxidoreductase
Also acts on UDP-alpha-D-2-deoxyglucose.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-26-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
UDP-glucose + 3-pyridinealdehyde adenine dinucleotide
UDP-glucuronate
-
-
-
?
UDP-glucose + nicotinamide hypoxanthine dinucleotide + H2O
UDP-glucuronate + ?
-
-
-
?
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+
-
-
-
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-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+
-
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+
-
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+
-
C276 is an active catalytic residue and critically involved in the substrate binding
-
?
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+
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 + 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 + 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
-
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
-
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 activity with uridine diphosphoacetylgalactosamine
-
?
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
?
-
-
no reaction with: 3-pyridinealdehyde deamino adenosine dinucleotide
-
?
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
-
?
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 ethylnicotinate adenine dinucleotide
-
?
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
-
?
additional information
?
-
-
no reaction with 3-formylpyridine adenine dinucleotide
-
?
additional information
?
-
-
thionicotinamide adenine dinucleotide
-
?
additional information
?
-
-
no reaction with 3-propionylpyridine adenine dinucleotide
-
?
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
-
?
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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+
-
-
-
?
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
-
delivers glucuronic acid for the formation of a antiphagocytic polysaccharide capsule that is required for virulence of pathogenic bacteria
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
cofactor binding triggers the formation of the 32 symmetry enzyme hexamer, which is the catalytically relevant state
additional information
-
no constantly bound chromophoric cofactors, i.e. NAD+, required
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
additional information
NaCl
is able to function in a variety of salt concentrations, enzymatic activity improves as salinity decreases. At 4 M NaCl concentration the enzyme was able to produce 870 nM NADH, while at 0.5 M NaCl, over 1.5 mM NADH is produced
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
gallic acid
-
is a non-competitive inhibitor with respect to UDP-glucose and NAD+. It decreases specific activities of UGDH, but does not affect UGDH protein expression, thus UGDH activity is inhibited by polyphenols at the post-translational level. Gallic acid exerts strong antiproliferative activity in breast cancer cells. Heat inactivation of UGDH is accelerated to a greater degree by quercetin than by gallic acid. In the presence of gallic acid, the activity remaining after 30 min is 55% that of control
NaCl
VNG1048G loses much of its activity when salinity drops below 3 M NaCl
NAD+
-
substrate inhibition, reversible by the addition of a nucleotide triphosphate, e.g. ATP, in the absence of kinase. Mutations in a previously identified UDP-glucuronic acid allosteric binding site decrease the binding affinity of the nucleotide triphosphate
quercetin
-
shows a competitive inhibition and a mixed-type inhibition with respect to UDP-glucose and NAD+, decreases specific activities of UGDH, but does not affect UGDH protein expression, thus UGDH activity is inhibited by polyphenols at the post-translational level. Quercetin exerts strong antiproliferative activity in breast cancer cells. Heat inactivation of UGDH is accelerated to a greater degree by quercetin than by gallic acid. In the presence of quercetin, the activity remaining after 30 min is 20% that of control
UDP-alpha-D-xylose
competitive. The DELTA132 deletion mutant and the UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces, suggesting that the hinge-bending motion represents a path for the allosteric transition between the different hexameric states
UDP-glucuronic acid
product inhibition, 44% residual activity at 1 mM; product inhibition, 79% residual activity at 1 mM
Uridine 5'-diphosphate chloroacetol
-
alkylates a thiol group of cysteine in the catalytic centre via being specifically bound instead of the substrate
NADH
-
0.1 mM, presence of 0.1 mM NAD+, 44% inhibition, presence of 0.5 mM NAD+, 6% inhibition
NADH
product inhibition, 26% residual activity at 0.05 mM; product inhibition, 70% residual activity at 0.05 mM
piperine
-
stronger inhibition with intestinal cell enzyme than with rat liver enzyme
piperine
-
non-competitive, reversible, non-pH-dependent, 90% inhibition at concentration 0.05 mM and 10% inhibition at concentration 0.01 mM
UDP-xylose
-
allosteric feedback inhibitor, reduces significantly the activity of the enzyme
additional information
-
the enzyme from serotype K30 is not inhibited by NAD+, in contrast to Escherichia coli K-12
-
additional information
-
no substrate inhibition, K+ is not inhibitory up to 500 mM, not inhibitory: dimethyldicarbonate, EDTA
-
additional information
-
in the presence of 0.12 mM 5-azido-UDP-glucose, 89% of the enzyme activity is lost after 5 min of photolabeling. When the enzyme is photolyzed in presence of 1 mM UDP-glucose, 11% of the enzyme activity is lost. 5-azido-UDP-glucose is photoinserting into a UDP-glucose-binding site on the human enzyme in a specific manner. Uracil, uridine, and glucose have a poor protective effect on the labeling, while UDP and UDP-glucose strongly inhibit photoinsertion
-
additional information
-
inhibition of human UDP-glucose dehydrogenase expression using siRNA expression vector in breast cancer cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17beta-estradiol
-
upregulation of UDP-glucose dehydrogenase at mRNA, protein and activity level in articular chondrocyte
lactose
-
UDP-GlcDH activities in extracts of Lactococcus lactis strain NFHA01 induced with both 0.5% and 2% lactose are significantly higher than that of the same strain without induction. UDP-GlcDH activity of NFHA01 induced with 2% lactose is about 110% higher than that of 0.5% lactose induction
nisin
-
induces the expression of szHasA together with szHasB
additional information
-
the enzyme shows a mechanism of activation that is NTP-dependent, poor activation by UDP-alpha-D-glucose. The inclusion of MgCl2 in the reaction buffer reverses the NTP-dependent activation of UgdK-12, in a concentration-dependent manner. This is not specific to Mg2+ as a similar effect is found for other divalent cations, including Ca2+, Mn2+, Zn2+, and Ni2+. Monovalent cations do not affect UgdK-12 activity. Chelating the divalent cation with EDTA or EGTA restores the NTP-dependent activation of UgdK-12
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Arthritis, Rheumatoid
Quantitative histochemical study of hyaluronic acid binding protein and the activity of uridine diphosphoglucose dehydrogenase in the synovium of patients with rheumatoid arthritis.
Arthritis, Rheumatoid
Uridine diphosphoglucose dehydrogenase activity in synovial lining cells in the experimental antigen induced model of rheumatoid arthritis: an indication of synovial lining cell function.
Brain Diseases
Loss-of-function mutations in UDP-Glucose 6-Dehydrogenase cause recessive developmental epileptic encephalopathy.
Breast Neoplasms
Correction: UDP-glucose 6-dehydrogenase regulates hyaluronic acid production and promotes breast cancer progression.
Breast Neoplasms
Identification and cloning of a novel androgen-responsive gene, uridine diphosphoglucose dehydrogenase, in human breast cancer cells.
Breast Neoplasms
Identification and Cloning of a Novel Androgen-Responsive Gene, Uridine Diphosphoglucose Dehydrogenase, in Human Breast Cancer Cells1.
Breast Neoplasms
Inhibition of Human UDP-Glucose Dehydrogenase Expression Using siRNA Expression Vector in Breast Cancer Cells
Breast Neoplasms
Inhibition of human UDP-glucose dehydrogenase expression using siRNA expression vector in breast cancer cells.
Breast Neoplasms
UDP-glucose 6-dehydrogenase knockout impairs migration and decreases in vivo metastatic ability of breast cancer cells.
Breast Neoplasms
UDP-glucose 6-dehydrogenase regulates hyaluronic acid production and promotes breast cancer progression.
Colorectal Neoplasms
Down-regulation of UDP-glucose dehydrogenase affects glycosaminoglycans synthesis and motility in HCT-8 colorectal carcinoma cells.
Granuloma
[Adrenocortical hormones and biosynthesis of acid mucopolysaccharides. II. UDPG:NAD oxidoreductase activity in the subcutaneous granuloma of adrenalectomized rats treated with cortisone, corticosterone and aldosterone]
Granulomatous Disease, Chronic
Discovery and Biochemical Characterization of UDP-Glucose Dehydrogenase from Granulibacter bethesdensis.
Graves Disease
Divergent Sp1 protein levels may underlie differential expression of UDP-glucose dehydrogenase by fibroblasts: role in susceptibility to orbital Graves disease.
Liver Neoplasms
Biochemical and histochemical properties of hepatic tumors of rainbow trout, Oncorhynchus mykiss.
Neoplasm Metastasis
Targeting UDP-glucose dehydrogenase inhibits ovarian cancer growth and metastasis.
Osteoarthritis
UDP-glucose dehydrogenase modulates proteoglycan synthesis in articular chondrocytes: its possible involvement and regulation in osteoarthritis.
Ovarian Neoplasms
Targeting UDP-glucose dehydrogenase inhibits ovarian cancer growth and metastasis.
Periodontitis
[UDP-glucose dehydrogenase and beta-glucuronidase activities in the gingival tissue of dogs with experimental periodontitis (author's transl)]
Prostatic Neoplasms
UDP-glucose dehydrogenase as a novel field-specific candidate biomarker of prostate cancer.
Rheumatoid Nodule
Palisading cells of rheumatoid nodules: comparison with synovial intimal cells.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35 - 0.62
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme, from different strains
0.35 - 0.62
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme, with 0.025-1.0 mM ATP
0.015
UDP-alpha-D-glucose
pH 7.4, 37°C, recombinant His-tagged mutant T325D
0.034
UDP-alpha-D-glucose
pH 7.4, 37°C, recombinant His-tagged wild-type enzyme
0.048
UDP-alpha-D-glucose
pH 7.4, 37°C, recombinant His-tagged mutant T325A
0.23
UDP-alpha-D-glucose
wild-type, pH 8.7, 30°C, Hill-coefficient 0.89
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 kinetic, cooperative kinetic behavior occurs in the hexameric enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.4 - 7.1
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme, from different strains
56.2
NAD+
-
pH 9.5, 37°C, recombinant wild-type enzyme, with 0.025-1.0 mM ATP
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000143
purified dodecameric enzyme, pH 9.2, temperature not specified in the publication
additional information
additional information
-
14.0, 1 unit is defined as the amount of enzyme required to produce 0.0002 mM of NADH per min at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
8.6
8.7
9.2
9.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
half-maximal activity at about pH 7.0 and pH 9.5, maximal activity at pH 8.0
9.5 - 11
pH 9.5: about 40% of maximal activity, pH 11.0: about 10% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 50
purified recombinant His-tagged enzyme, activity range, profile overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
originally isolated from the lymph nodes of patients with chronic granulomatous disease (CGD)
-
-
brenda
two-dimensional IEF SDS-PAGE showed several isoforms of the purified enzyme
-
-
brenda
induction by short-term feeding with sucrose, sorbitol, ethylene glycol or light exposure
SwissProt
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
overexpression of enzyme plus transformation of gene cluster for K5 polysaccharide production
-
-
brenda
isoform PA3559, expressed primarily in low concentrations of Mg2+
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
silencing of UGDH decreases glycosaminoglycan synthesis causing severe embryonic malformations because of defective gastrulation process. Overexpression of the enzyme from Xenopus laevis in human smooth muscle cells increases the accumulation of hyaluronan
brenda
-
enzyme activity depends on growth phase of the culture
brenda
the abundance of enzyme mRNA in pistils is more than 3fold greater than that in other parts, and the abundance in stamens and calyx tubes is relatively high compared with that in sepals and petals
brenda
changes in the mRNA level during peach fruit development correspond to changes in the amount of cell wall material and the cell wall uronic acid content. These are greater in the fruits of the commercial cultivars compared with the Japanese native peach cultivars, and the expression of enzyme is higher in the fruits of the commercial cultivars
brenda
-
increased UGDH expression in cancerous acini and decreased expression in normal-appearing acini of the same prostate relative to acini of non-cancerous prostates
brenda
enzyme activity increases dramatically in a special subset of vulval cells during vulval morphogenesis
brenda
-
siRNA for the human enzyme is put into a pRNA-U6.1/Neo vector and chemically transfected into bresat cancer cells. The UGDH siRNA plasmid then knocks down UGDH expression in ZR-75-1 cells
brenda
additional information
-
overexpression of c-Krox in articular chondrocytes depresses both UDPGD mRNA steady-state level and protein expression
brenda
the level of mRNA in immature leaves is much higher than that in mature leaves
brenda
additional information
the organism grows optimally in 3-5 M NaCl, requiring the higher salinity for proper growth and cell shape
brenda
additional information
-
the organism grows optimally in 3-5 M NaCl, requiring the higher salinity for proper growth and cell shape
brenda
additional information
-
the organism grows optimally in 3-5 M NaCl, requiring the higher salinity for proper growth and cell shape
brenda
additional information
the organism grows optimally in 1.7-2.5 M NaCl
brenda
additional information
-
the organism grows optimally in 1.7-2.5 M NaCl
brenda
additional information
-
the organism grows optimally in 1.7-2.5 M NaCl
brenda
additional information
the LgUGDH gene is expressed in all larch plant organs, primarily in the larch stems, in addition to its roots and leaves
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
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
-
UGDH protein level in rat osteoarthritis cartilage are much lower than the corresponding controls and negatively correlated to the degree of osteoarthritis
malfunction
-
Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
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
-
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
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
-
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
-
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
-
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
-
UGDH is essential in the proteoglycan synthesis in articular chondrocytes, overview
physiological function
Streptococcus pyogenes M1 GAS 5448
-
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 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 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 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
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
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
-
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
-
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
-
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
-
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
-
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
Show AA Sequence and Transmembrane Helices (41312 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
300000
340000
44000
47000
48500
50000
52000
550000
57000
52000
-
6 * 52000, at pH 5.5-7.8, equilibrium measurement under native and denaturing conditions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dodecamer
hexamer
homodimer
monomer
tetramer
additional information
?
x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE
?
-
x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE
hexamer
-
6 * 52000, at pH 5.5-7.8, equilibrium measurement under native and denaturing conditions
homodimer
recombinant form of Ugd(BCAL2946)
homodimer
recombinant form of Ugd(BCAM0855)
additional information
-
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
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
-
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
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