Information on EC 1.1.1.22 - UDP-glucose 6-dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.1.1.22
-
RECOMMENDED NAME
GeneOntology No.
UDP-glucose 6-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
ping-pong reaction mechanism
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
also shows alcohol dehydrogenase activity
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
also shows alcohol dehydrogenase activity; also shows aldehyde dehydrogenase activity; 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+
show the reaction diagram
two-step reaction, reaction mechanism
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
bi-uni-uni-bi mechanism
Saccharum spp.
-
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
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+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Ascorbate and aldarate metabolism
-
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Pentose and glucuronate interconversions
-
Starch and sucrose metabolism
-
UDP-alpha-D-glucuronate biosynthesis (from UDP-glucose)
-
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:NAD+ 6-oxidoreductase
Also acts on UDP-alpha-D-2-deoxyglucose.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ADH-like UDP-glucose dehydrogenase
Q6IVK8
-
BceC
Burkholderia cepacia IST408
-
-
-
dehydrogenase, uridine diphosphoglucose
-
-
-
-
dual specificity UDP-glucose dehydrogenase
Q6IVK8
-
HasB
Streptococcus pyogenes 5448
P0C0F5
-
-
HasB2
Streptococcus pyogenes 5448
Q490A1
-
-
PA2022
O86422
-
PA3559
Q9HY58
-
Sugarless protein
-
-
-
-
UDP-alpha-D-glucose:NAD oxidoreductase
-
-
-
-
UDP-D-glucose dehydrogenase
-
-
-
-
UDP-GDH
A1RUM9
-
UDP-Glc dehydrogenase
-
-
-
-
UDP-Glc DH
-
-
-
-
UDP-GlcDH
-
-
-
-
UDP-GlcDH
Streptococcus equi subsp. zooepidemicus FHA0
-
-
-
UDP-GlcDHase
B5L017
-
UDP-GlcDHase
Phoma herbarum YS4108
B5L017
-
-
UDP-glucose dehydrogenase
Q9FM01, Q9LF33, Q9LIA8, Q9MAB5
-
UDP-glucose dehydrogenase
B4EB36, B4EMQ8, B4EN77
-
UDP-glucose dehydrogenase
-
-
UDP-glucose dehydrogenase
Burkholderia cepacia IST408
-
-
-
UDP-glucose dehydrogenase
-
-
UDP-glucose dehydrogenase
C3VI43
-
UDP-glucose dehydrogenase
A1RUM9
-
UDP-glucose dehydrogenase
A4UTT2
-
UDP-glucose dehydrogenase
A4UTT2
-
-
UDP-glucose dehydrogenase
-
-
UDP-glucose dehydrogenase
Streptococcus equi subsp. zooepidemicus FHA0
-
-
-
UDPG dehydrogenase
-
-
-
-
UDPG:NAD oxidoreductase
-
-
-
-
UDPGDH
-
-
-
-
UDPGDH
Q6IVK8
-
UDPGDH
-
-
UDPGDH-A
-
-
UDPGDH-B
-
-
UDPGlc dehydrogenase
-
-
-
-
UDPglucose dehydrogenase
-
-
-
-
UDPglucose:NAD+ oxidoreductase
-
-
-
-
Ugd
B4EB36, B4EMQ8, B4EN77
-
Ugd
C3VI43
-
UGD1
L0N5L6
-
UgdG
A4UTT2
-
UGDH
O60701
-
UGDH
Q56R95
-
uridine diphosphate D-glucose dehydrogenase
-
-
-
-
uridine diphosphate glucose dehydrogenase
-
-
-
-
uridine diphosphate glucose-6-dehydrogenase
-
-
uridine diphosphate-glucose dehydrogenase
-
-
uridine diphosphoglucose dehydrogenase
-
-
-
-
uridine-5'-diphosphoglucose dehydrogenase
-
-
uridine-5'-diphosphoglucose dehydrogenase
Burkholderia cepacia IST408
-
-
-
uridyl phosphate dehydrogenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-26-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
Burkholderia cepacia IST408
gene bceC
-
-
Manually annotated by BRENDA team
overexpression of enzyme plus transformation of gene cluster for K5 polysaccharide production
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
chemically synthesized gene expressed in Escherichia coli
UniProt
Manually annotated by BRENDA team
recombinant His-tagged enzyme
UniProt
Manually annotated by BRENDA team
cultivar NVS or K326
SwissProt
Manually annotated by BRENDA team
two-dimensional IEF SDS-PAGE showed several isoforms of the purified enzyme
-
-
Manually annotated by BRENDA team
Phoma herbarum YS4108
-
UniProt
Manually annotated by BRENDA team
induction by short-term feeding with sucrose, sorbitol, ethylene glycol or light exposure
SwissProt
Manually annotated by BRENDA team
gene ugd
UniProt
Manually annotated by BRENDA team
strain PAO1, isoform PA2022, constitutively expressed
SwissProt
Manually annotated by BRENDA team
strain PAO1, isoform PA3559, expressed primarily in low concentrations of Mg2+
SwissProt
Manually annotated by BRENDA team
Saccharum spp.
hybrid
-
-
Manually annotated by BRENDA team
gene ugdG
UniProt
Manually annotated by BRENDA team
strain ATCC 31461
-
-
Manually annotated by BRENDA team
Streptococcus equi subsp. zooepidemicus FHA0
FHA0
-
-
Manually annotated by BRENDA team
isoform HasB
UniProt
Manually annotated by BRENDA team
isoform HasB2
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes 5448
isoform HasB
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes 5448
isoform HasB2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
A4UTT2
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
P0C0F5, Q490A1
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; 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
-
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
Streptococcus pyogenes 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; 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
C3VI43, -
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-OH-benzopyrene + NAD+
?
show the reaction diagram
-
-
-
-
?
5-azido-UDP-glucose + NAD+
5-azido-UDP-glucuronate + NADH + H+
show the reaction diagram
-
-
-
-
?
5-fluorouracil + NAD+
?
show the reaction diagram
-
-
-
-
?
6-azauracil + NAD+
?
show the reaction diagram
-
-
-
-
?
CDP-glucose + NAD+ + H2O
CDP-glucuronate + NADH
show the reaction diagram
-
17% of the reaction rate with UDP-glucose
-
-
?
CDP-glucose + NAD+ + H2O
CDP-glucuronate + NADH
show the reaction diagram
-
reaction rate is 5.5% of that with UDP-glucose
-
-
?
CTP-glucose + NAD+
CTP-glucuronate + NADH
show the reaction diagram
Saccharum spp.
-
8% of activity with UDP-glucose
-
-
ir
TDP-glucose + NAD+
TDP-glucuronate + NADH
show the reaction diagram
Saccharum spp.
-
2% of activity with UDP-glucose
-
-
ir
TDP-glucose + NAD+ + H2O
TDP-glucuronate + NADH
show the reaction diagram
-
reaction rate is 17% of that with UDPglucose
-
-
?
TDP-glucose + NAD+ + H2O
TDP-glucuronate + NADH
show the reaction diagram
O86422, -, Q9HY58
38.5% of the rate with UDP-glucose
-
-
?
UDP-2-deoxy-D-glucose + NAD+ + H2O
UDP-2-deoxy-D-glucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
B5L017
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-, C9E261
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
P0C0F5, Q490A1
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
Streptococcus pyogenes 5448
P0C0F5, Q490A1
-
-
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
Phoma herbarum YS4108
B5L017
-
-
-
?
UDP-galactose + NAD+ + H2O
UDP-galacturonate + NADH
show the reaction diagram
O86422, -, Q9HY58
11.9% of the rate with UDP-glucose
-
-
?
UDP-galactose + NAD+ + H2O
UDP-galacturonate + NADH
show the reaction diagram
O86422, -, Q9HY58
6.4% of the rate with UDP-glucose
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
O60701
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
Saccharum spp.
-
-
-
-
ir
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
O60701
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-, Q19905
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
Q56R95, -
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
O86422, -, Q9HY58
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
reversal of reaction cannot be demonstrated
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
NADP+, about 1% of activity of NAD+
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
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+
show the reaction diagram
Q56R95, -
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+
show the reaction diagram
-
UDPGDH-A activity has a more important role than UDPGDH-B in synthesis of UDP-glucuronate
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
C276 is an active catalytic residue and critically involved in the substrate binding
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-, Q6IVK8
the enzyme has dual specificity with UDP-glucose and ethanol
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
B4EB36, B4EMQ8, B4EN77
recombinant forms Ugd(BCAL2946) and Ugd(BCAM0855) have similar in vitro Ugd activity
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
Streptococcus equi subsp. zooepidemicus FHA0
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
A4UTT2
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
C3VI43, -
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
Burkholderia cepacia IST408
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
A4UTT2
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
show the reaction diagram
-
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
show the reaction diagram
-
-
-
-
?
UDP-glucose + 3-acetylpyridine adenine dinucleotide + H2O
UDP-glucuronate + ?
show the reaction diagram
-
-
-
-
-
UDP-glucose + 3-pyridinealdehyde adenine dinucleotide
UDP-glucuronate
show the reaction diagram
-
-
-
-
?
UDP-glucose + deamino adenine dinucleotide + H2O
UDP-glucuronate + ?
show the reaction diagram
-
-
-
-
?
UDP-glucose + deamino adenine dinucleotide + H2O
UDP-glucuronate + ?
show the reaction diagram
-
-
-
-
?
UDP-glucose + nicotinamide hypoxanthine dinucleotide + H2O
UDP-glucuronate + ?
show the reaction diagram
-
-
-
-
?
UDP-glucose + thionicotinamide adenine dinucleotide + H2O
UDP-glucuronate + ?
show the reaction diagram
-
-
-
-
?
UDP-glucose + thionicotinamide adenine dinucleotide + H2O
UDP-glucuronate + ?
show the reaction diagram
-
-
-
-
-
UDP-N-acetylglucosamine + NAD+ + H2O
? + NADH
show the reaction diagram
O86422, -, Q9HY58
35% of the rate with UDP-glucose
-
-
?
UDP-N-acetylglucosamine + NAD+ + H2O
? + NADH
show the reaction diagram
O86422, -, Q9HY58
6.3% of the rate with UDP-glucose
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
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
show the reaction diagram
-
delivers glucuronic acid for the formation of a antiphagocytic polysaccharide capsule that is required for virulence of pathogenic bacteria
-
-
?
dTDP-glucose + NAD+ + H2O
dTDP-glucuronate + NADH
show the reaction diagram
-
reaction rate is 16.7% of that with UDPglucose
-
-
?
additional information
?
-
-
no reaction with ethylnicotinate adenine dinucleotide
-
-
-
additional information
?
-
-
nicotinamide hypoxanthine dinucleotide
-
-
-
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
cosubstrates which can replace NAD+: 3-acetylpyridine 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 alpha-NAD+
-
-
-
additional information
?
-
-
3-pyridinealdehyde adenine dinucleotide
-
-
-
additional information
?
-
-
no reaction with 3-formylpyridine adenine dinucleotide
-
-
-
additional information
?
-
-
no reaction with NADP+
-
-
-
additional information
?
-
-
no reaction with NADP+
-
-
-
additional information
?
-
-
thionicotinamide adenine dinucleotide
-
-
-
additional information
?
-
-
thionicotinamide adenine dinucleotide
-
-
-
additional information
?
-
-
no activity with GTP-glucose, no reaction with: 3-pyridinealdehyde deamino adenosine dinucleotide
-
-
-
additional information
?
-
-
no activity with glucose
-
-
-
additional information
?
-
-
deamino adenine dinucleotide
-
-
-
additional information
?
-
-
deamino adenine dinucleotide, no activity with uridine diphosphoacetylgalactosamine, no activity with ethyl alcohol
-
-
-
additional information
?
-
-
no reaction with deamino-NAD+
-
-
-
additional information
?
-
-
no activity with alpha-D-glucose-1-phosphate, no activity with guanosine diphosphomannose, no activity with uridine diphosphoacetylglucosamine
-
-
-
additional information
?
-
-
no activity with ADP-glucose
-
-
-
additional information
?
-
-
no reaction with 3-propionylpyridine adenine dinucleotide
-
-
-
additional information
?
-
Saccharum spp.
-
no substrate: ADP-glucose
-
-
-
additional information
?
-
-
no substrate: UDP-galactose, UDP-N-galactosamin, ADP-glucose, GDP-glucose, GDP-mannose
-
-
-
additional information
?
-
-
no substrate: ADP-glucose, TDP-glucose
-
-
-
additional information
?
-
B4EB36, B4EMQ8, B4EN77
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
?
-
B4EB36, B4EMQ8, B4EN77
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
?
-
-
importance of both UDPDH and mshA gene expression for successful light organ colonization in the sepiolid squid Euprymna tasmanica
-
-
-
additional information
?
-
B4EB36, B4EMQ8, B4EN77
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
?
-
-
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
?
-
-
no substrates: UDP-D-galactose, UTP, 5'-UMP and D-galactose
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronate + 2 NADH + 2 H+
show the reaction diagram
-
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+
show the reaction diagram
Q56R95, -
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+
show the reaction diagram
-
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+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
A4UTT2
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
C3VI43, -
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
Burkholderia cepacia IST408
-
-
-
-
?
UDP-glucose + 2 NAD+ + H2O
UDP-glucuronic acid + 2 NADH + 2 H+
show the reaction diagram
A4UTT2
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
-
-
-
?
UDPglucose + NAD+ + H2O
UDPglucuronate + NADH
show the reaction diagram
-
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
show the reaction diagram
-
delivers glucuronic acid for the formation of a antiphagocytic polysaccharide capsule that is required for virulence of pathogenic bacteria
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
can replace NAD+
3-acetylpyridine adenine dinucleotide
-
can replace NAD+
3-acetylpyridine adenine dinucleotide
-
can replace NAD+
NAD+
-
specific for
NAD+
Saccharum spp.
-
-
NAD+
Q56R95, -
-
NAD+
-
activity with NADP+ is about 20% of that with NAD+
NAD+
-
cofactor binding triggers the formation of the 32 symmetry enzyme hexamer, which is the catalytically relevant state
NADP+
-
activity with NADP+ is about 20% of that with NAD+
NADP+
-
about 5-12% of the activity with NAD+
additional information
-
no constantly bound chromophoric cofactors, i.e. NAD+, required
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
no metal ion requirement
additional information
-
no metal ion requirement
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ca2+
O86422, -, Q9HY58
84% residual activity at 1 mM
EDTA
O86422, -, Q9HY58
83% residual activity at 1 mM
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
NADH
-
0.1 mM, presence of 0.1 mM NAD+, 44% inhibition, presence of 0.5 mM NAD+, 6% inhibition
NADH
O86422, -, Q9HY58
product inhibition, 26% residual activity at 0.05 mM; product inhibition, 70% residual activity at 0.05 mM
NADH
-
0.05 mM, partial inhibition
NH2OH
-
deactivation
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
0.001 mM, 66% inhibition
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
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
thiol group modifying reagents
-
-
-
UDP
-
0.5 mM, partial inhibition
UDP-alpha-D-glucuronate
-
0.05 mM, partial inhibition
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-D-galactose
-
slight
UDP-D-xylose
-
competitive with UDPglucose
UDP-D-xylose
-
-
UDP-D-xylose
-
competitive with UDPglucose
UDP-galactose
-
0.5 mM, partial inhibition
UDP-glucuronate
Saccharum spp.
-
competitive
UDP-glucuronic acid
O86422, -, Q9HY58
product inhibition, 44% residual activity at 1 mM; product inhibition, 79% residual activity at 1 mM
UDP-xylose
Saccharum spp.
-
competitive
UDP-xylose
-
0.05 mM, partial inhibition
UDPgalacturonic acid
-
-
UDPglucuronate
-
-
UDPglucuronate
-
-
UDPglucuronate
-
-
UDPglucuronate
-
product feed-back inhibition competitive with UDPglucose
UDPglucuronate
-
product feed-back inhibition competitive with UDPglucose
Uridine 5'-diphosphate chloroacetol
-
alkylates a thiol group of cysteine in the catalytic centre via being specifically bound instead of the substrate
Mn2+
O86422, -, Q9HY58
84% residual activity at 1 mM
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
17beta-estradiol
-
upregulation of UDP-glucose dehydrogenase at mRNA, protein and activity level in articular chondrocyte
3-pyridinealdehyde adenine dinucleotide
-
can replace NAD+
Deamino adenine dinucleotide
-
can replace NAD+
Deamino adenine dinucleotide
-
can replace NAD+
nicotinamide hypoxanthine dinucleotide
-
can replace NAD+
nisin
-
induces the expression of szHasA together with szHasB
TGF-beta
-
enhances enzyme activity in articular chondrocyte
-
Thionicotinamide adenine dinucleotide
-
can replace NAD+
Thionicotinamide adenine dinucleotide
-
can replace NAD+
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
additional information
-
fetal calf serum stimulates enzyme activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.05617
-
5-azido-UDP-glucose
-
22C, pH 8.7
0.006
-
NAD+
-
37C, pH 10.5
0.042
-
NAD+
-
isoform Ugd3, pH 8.7, 22C
0.043
-
NAD+
-
isoform Ugd2, pH 8.7, 22C
0.044
-
NAD+
-
isoform Ugd4, pH 8.7, 22C
0.05
-
NAD+
-
-
0.065
-
NAD+
-
wild-type
0.07
-
NAD+
-
pH 8.7, 25C
0.0722
-
NAD+
Saccharum spp.
-
pH 8.4, 25C
0.1
-
NAD+
-
mutant E161Q, pH 8.7, 25C
0.13
-
NAD+
-
-
0.132
-
NAD+
-
pH 8.8, 25C
0.133
-
NAD+
O60701
pH 8.7, 25C
0.133
-
NAD+
-
wild-type, pH 8.7, 22C
0.135
-
NAD+
-
mutant E141Q
0.16
-
NAD+
-
50C, pH 10.5
0.168
-
NAD+
B5L017
pH 8.4, 30C
0.17
-
NAD+
-
-
0.17
-
NAD+
B4EB36, B4EMQ8, B4EN77
-
0.187
-
NAD+
-
mutant E145Q
0.2
-
NAD+
-, Q19905
pH 8.7, 22C
0.21
-
NAD+
B4EB36, B4EMQ8, B4EN77
-
0.3
-
NAD+
Q56R95, -
-
0.355
-
NAD+
O60701
pH 7.4, 22C
0.384
-
NAD+
-
wild-type, pH 8.7, 25C
0.4
-
NAD+
-
mutant T118A
0.4
-
NAD+
-
pH 8.7, 30C
0.401
-
NAD+
-
mutant A222Q/S233G, pH 8.7, 22C
0.42
-
NAD+
-
wild-type, pH 7.4, 22C
0.47
-
NAD+
O86422, -, Q9HY58
pH 7.5, 22C
0.53
-
NAD+
-
mutant K339A, pH 7.4, 22C
0.53
-
NAD+
-, C9E261
wild-type, pH 8.7, 30C, Hill-coefficient 1.5
0.69
-
NAD+
-
70C, pH 10.5
0.7
-
NAD+
-
wild-type, pH 8.7, 25C
0.942
-
NAD+
-
wild-type, pH 7.5, 25C, Hill coefficient 0.74
1.99
-
NAD+
O86422, -, Q9HY58
pH 7.5, 22C
2.1
-
NAD+
-
mutant K339A, pH 7.4, 22C
2.92
-
NAD+
-
mutant K94E, pH 7.5, 25C
6.3
-
NAD+
-
mutant K94E, pH 8.7, 25C
0.017
-
UDP
-
wild-type, pH 8.7, 22C
0.98
-
UDP
-
mutant A222Q/S233G, pH 8.7, 22C
0.016
-
UDP-alpha-D-glucose
-
wild-type, pH 7.5, 25C
0.021
-
UDP-alpha-D-glucose
-
pH 8.8, 25C
0.025
-
UDP-alpha-D-glucose
-
wild-type, pH 8.7, 25C
0.035
-
UDP-alpha-D-glucose
-
wild-type, pH 8.7, 25C
0.055
-
UDP-alpha-D-glucose
-
mutant E161Q, pH 8.7, 25C
0.0958
-
UDP-alpha-D-glucose
B5L017
pH 8.4, 30C
0.23
-
UDP-alpha-D-glucose
-, C9E261
wild-type, pH 8.7, 30C, Hill-coefficient 0.89
0.269
-
UDP-alpha-D-glucose
-
mutant K94E, pH 7.5, 25C
0.32
-
UDP-alpha-D-glucose
-
37C, pH 10.5
0.42
-
UDP-alpha-D-glucose
-
50C, pH 10.5
1.28
-
UDP-alpha-D-glucose
-
70C, pH 10.5
2.21
-
UDP-alpha-D-glucose
-
mutant K94E, pH 8.7, 25C
0.0092
-
UDP-glucose
-
wild-type, pH 7.4, 22C
0.011
-
UDP-glucose
O60701
pH 7.4, 22C
0.017
-
UDP-glucose
O60701
pH 8.7, 25C
0.017
-
UDP-glucose
-
-
0.01703
-
UDP-glucose
-
22C, pH 8.7
0.0187
-
UDP-glucose
Saccharum spp.
-
pH 8.4, 25C
0.02
-
UDP-glucose
-
wild-type
0.02
-
UDP-glucose
B4EB36, B4EMQ8, B4EN77
;
0.022
-
UDP-glucose
-
pH 8.7, 25C
0.022
-
UDP-glucose
-
mutant K339A, pH 7.4, 22C
0.059
-
UDP-glucose
-
mutant T118A
0.06
-
UDP-glucose
-
mutant E141Q
0.12
-
UDP-glucose
O86422, -, Q9HY58
pH 7.5, 22C
0.123
-
UDP-glucose
-
isoform Ugd2, pH 8.7, 22C
0.125
-
UDP-glucose
-
mutant E145Q
0.171
-
UDP-glucose
-
isoform Ugd4, pH 8.7, 22C
0.2
-
UDP-glucose
-, Q19905
pH 8.7, 22C
0.335
-
UDP-glucose
-
isoform Ugd3, pH 8.7, 22C
0.38
-
UDP-glucose
-
20C, pH 8, UDPGDH-A
0.4
-
UDP-glucose
O86422, -, Q9HY58
pH 7.5, 22C
0.87
-
UDP-glucose
-
pH 8.7, 30C
0.9
-
UDP-glucose
Q56R95, -
-
0.95
-
UDP-glucose
-
20C, pH 8, UDPGDH-B
1.5
-
UDP-glucose
-
mutant K339A, pH 7.4, 22C
0.015
-
UDPglucose
-
pH 9.4
0.02
-
UDPglucose
-
-
0.035
-
UDPglucose
-
pH 8.6
0.05
-
UDPglucose
-
-
0.0756
-
UDPglucose
-
native enzyme
0.108
-
UDPglucose
-
-
0.3
-
UDPglucose
-
-
1
-
UDPglucose
-
-
1
-
UDPglucose
-
dissociated enzyme
5.5
-
UDPglucose
-
-
6.6
-
UDPglucose
-
-
8.4
-
UDPglucose
-
recombinant glutathione-S-transferase fusion protein
0.058
-
aldehyde intermediate
-
-
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.9
-
aldehyde intermediate
-
-
-
0.02
-
NAD+
-
mutant K94E, pH 8.7, 25C
0.055
-
NAD+
-
mutant K94E, pH 7.5, 25C
0.154
-
NAD+
B4EB36, B4EMQ8, B4EN77
-
0.156
-
NAD+
B4EB36, B4EMQ8, B4EN77
-
0.37
-
NAD+
O86422, -, Q9HY58
pH 7.5, 22C
1.8
-
NAD+
-
wild-type, pH 7.5, 25C, Hill coefficient 0.74
2.35
-
NAD+
O86422, -, Q9HY58
pH 7.5, 22C
4.4
-
NAD+
-
wild-type, pH 8.7, 25C
6.7
-
NAD+
-, C9E261
wild-type, pH 8.7, 30C
7.6
-
NAD+
-
pH 8.7, 30C
97
-
UDP
-
mutant A222Q/S233G, pH 8.7, 22C
105
-
UDP
-
wild-type, pH 8.7, 22C
0.0014
-
UDP-alpha-D-glucose
-
mutant E161Q, pH 8.7, 25C
0.012
-
UDP-alpha-D-glucose
-
mutant K94E, pH 7.5, 25C
0.02
-
UDP-alpha-D-glucose
-
mutant K94E, pH 8.7, 25C
0.85
-
UDP-alpha-D-glucose
-
wild-type, pH 8.7, 25C
1.4
-
UDP-alpha-D-glucose
-
wild-type, pH 7.5, 25C
3.2
-
UDP-alpha-D-glucose
-
wild-type, pH 8.7, 25C
6.9
-
UDP-alpha-D-glucose
-, C9E261
wild-type, pH 8.7, 30C
0.127
-
UDP-glucose
B4EB36, B4EMQ8, B4EN77
-
0.133
-
UDP-glucose
B4EB36, B4EMQ8, B4EN77
-
0.24
-
UDP-glucose
O86422, -, Q9HY58
pH 7.5, 22C
0.81
-
UDP-glucose
O86422, -, Q9HY58
pH 7.5, 22C
1.17
-
UDP-glucose
-
isoform Ugd4, pH 8.7, 22C
1.92
-
UDP-glucose
-
isoform Ugd2, pH 8.7, 22C
2.53
-
UDP-glucose
-
isoform Ugd3, pH 8.7, 22C
8.73
-
UDP-glucose
-
pH 8.7, 30C
0.117
-
UDPglucose
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.014
-
NAD+
-
mutant E161Q, pH 8.7, 25C
14330
1.2
-
NAD+
-
wild-type, pH 8.7, 25C
14330
0.025
-
UDP-alpha-D-glucose
-
mutant E161Q, pH 8.7, 25C
219166
24
-
UDP-alpha-D-glucose
-
wild-type, pH 8.7, 25C
219166
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.744
-
Gallic acid
-
with respect to UDP-glucose
1.804
-
Gallic acid
-
with respect to NAD+
0.0005
-
p-chloromercuribenzoate
-
pH 8.7, 25C
0.07
-
quercetin
-
with respect to NAD+
0.083
-
quercetin
-
with respect to UDP-glucose
0.292
-
UDP-glucuronate
Saccharum spp.
-
pH 8.4, 25C
0.017
-
UDP-xylose
Saccharum spp.
-
pH 8.4, 25C
0.083
-
UDP-xylose
-
isoform Ugd2, pH 8.7, 22C
0.16
-
UDP-xylose
-
isoform Ugd3, pH 8.7, 22C
0.22
-
UDP-xylose
-
isoform Ugd4, pH 8.7, 22C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.1e-05
-
-
mutant D280N, pH 7.4, 22C
0.00022
-
-
mutant K276A, pH 7.4, 22C
0.0004
-
-
mutant K220H, pH 7.4, 22C
0.00041
-
-
mutant K220R, pH 7.4, 22C
0.00051
-
-
lysates of cells treated with 0.3 mM gallic acid
0.00061
-
-
lysates of cells treated with 0.3 mM quercetin
0.0015
-
-
control lysates
0.00247
-
-
mutant K279A, pH 7.4, 22C
0.0027
-
-
mutant K276S, pH 7.4, 22C
0.0029
-
-
mutant K220A, pH 7.4, 22C
0.00299
-
-, Q6IVK8
-
0.41
-
-
mutant D280E, pH 7.4, 22C
0.69
-
-
wild-type, 22C, pH 7.4
0.74
-
-
mutant K339A, pH 7.4, 22C
1.5
-
-
recombinant and purified
2.17
-
Saccharum spp.
-
pH 8.4, 25C
27.17
-
-
purified 390fold
342.9
-
-
pH 8.8, 25C
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 30C
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.4
-
Saccharum spp.
-
-
8.4
-
-
-
8.6
-
-
two pH optima, pH 8.6 and pH 9.4
8.6
-
B5L017
-
8.7
-
-
-
8.7
-
-
-
8.7
-
-, C9E261
-
9.4
-
-
two pH optima, pH 8.6 and pH 9.4
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
11
B5L017
no enzymic activity beyond
6.3
8.6
-
at pH 6.3 and 8.6 about 50% of activity maximum
7
9.5
-
-
7
-
-
46% of maximum acitivity
7
-
-, C9E261
37% of maximum activity
7.5
9.4
-
at pH 7.5 and 9.4 about 50% of activity maximum
7.8
9.4
-
at pH 7.8 and 9.4 about 50% of activity maximum
8.8
-
-
80-83% of maximum activity
9.5
11
-
pH 9.5: about 40% of maximal activity, pH 11.0: about 10% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
45
-
-
30
-
-
assay at
30
-
-
-
30
-
-, C9E261
-
35
-
B5L017
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-, C9E261
significant decrease in activity below
30
-
-
90% of maximum activity
40
-
-, C9E261
70% of maximum activity
50
-
B5L017
no enzymic activity above
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
overexpression of c-Krox in articular chondrocytes depresses both UDPGD mRNA steady-state level and protein expression
Manually annotated by BRENDA team
-
articular chondrocyte
Manually annotated by BRENDA team
Q56R95, -
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
Manually annotated by BRENDA team
-
enzyme activity depends on growth phase of the culture
Manually annotated by BRENDA team
L0N5L6
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
Manually annotated by BRENDA team
L0N5L6
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
Manually annotated by BRENDA team
L0N5L6
the level of mRNA in immature leaves is much higher than that in mature leaves
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
prostate tumor cell line derived from PC-3 cells
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
increased UGDH expression in cancerous acini and decreased expression in normal-appearing acini of the same prostate relative to acini of non-cancerous prostates
Manually annotated by BRENDA team
Q9FM01, Q9LF33, Q9LIA8, Q9MAB5
-
Manually annotated by BRENDA team
Q9FM01, Q9LF33, Q9LIA8, Q9MAB5
-
Manually annotated by BRENDA team
Saccharum spp.
-
-
Manually annotated by BRENDA team
-, Q19905
enzyme activity increases dramatically in a special subset of vulval cells during vulval morphogenesis
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant fusion protein
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
44000
-
-
gel filtration
45500
-
-
electrospray mass spectrometry
50900
-
B4EB36, B4EMQ8, B4EN77
Ugd-FLAG-BCAM2034
51700
-
B4EB36, B4EMQ8, B4EN77
Ugd-FLAG-BCAL2946
52000
-
-
gel filtation
52100
-
B4EB36, B4EMQ8, B4EN77
Ugd-FLAG-BCAM0855
55000
-
-
gel filtration
57000
-
-
gel filtration, minor part of wild-type
72000
-
-
gel filtration
86000
-
-
gel filtration
104000
-
O86422, -, Q9HY58
gel filtration
110000
-
-
gel filtration, minor part of wild-type, mutant A222Q/S233G
117000
-
O86422, -, Q9HY58
gel filtration
300000
-
-
gel filtration
300000
-
-
gel filtration
305000
-
-
equilibrium measurement under native conditions
340000
-
O60701
gel filtration
340000
-
-
gel filtration, wild-type
345000
-
O60701
gel filtration, dynamic light scattering
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
? * 40000, SDS-PAGE
?
Saccharum spp.
-
x * 52000, SDS-PAGE
?
Q9SQJ1
x * 53100, deduced from gene sequence
?
-, Q6IVK8
x * 43000, SDS-PAGE
?
-
x * 48500, SDS-PAGE and calculated for His-tagged protein
?
-
x * 52600, recombinant His6-tagged BceC, SDS-PAGE
?
P0C0F5, Q490A1
x * 42000, SDS-PAGE, x * 43400, calculated
?
B5L017
x * 56300, calculated, x * 60000, SDS-PAGE
?
Burkholderia cepacia IST408
-
x * 52600, recombinant His6-tagged BceC, SDS-PAGE
-
?
Phoma herbarum YS4108
-
x * 56300, calculated, x * 60000, SDS-PAGE
-
?
Streptococcus pyogenes 5448
-
x * 42000, SDS-PAGE, x * 43400, calculated
-
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 57000, mutant A222Q/S233G and part of wild-type, SDS-PAGE
dimer
O86422, -, Q9HY58
54500, calculated; 57400, calculated
hexamer
-
6 * 52000, at pH 5.5-7.8, equilibrium measurement under native and denaturing conditions
hexamer
-
6 * 52000, gel filtration
hexamer
O60701
6 x 57000, SDS-PAGE
hexamer
O60701
6 * 57000, SDS-PAGE
hexamer
-
6* 57000, wild-type, plus some dimer and monomer, SDS-PAGE
hexamer
-
6 * 50000, SDS-PAGE
homodimer
B4EB36, B4EMQ8, B4EN77
recombinant form of Ugd(BCAL2946); recombinant form of Ugd(BCAM0855)
monomer
-
1 * 45500, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 57000, SDS-PAGE, minor part of wild-type, major part is hexamer
tetramer
-
4 * 70000, gel filtration after treatment with SDS
tetramer
-
-
monomer
-
1 * 50000, SDS-PAGE
additional information
O60701
significant amount of dimeric and monomeric species can be detected
additional information
O60701
identification of amino acids I7 through T19 as NAD+ binding-site by photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant His6-tagged BceC, 0.001 ml of protein solution containing 5 mg/ml protein in 25 mM Tris-HCl, pH 8.3, 50 mM NaCl, 2.5 mM DTT, 0.25 mM UDP-GlcA, and 0.5 mM NAD+, is mixed with 0.001 ml of precipitant solution containing 200 mM ammonium sulfate, 100 mM sodium acetate, pH 4.5, 11% w/v PEG 4000, and 50 mM NaF, method optimiization, X-ray diffraction structure determination and analysis at 2.09 A resolution, molecular replacement
-
to 1.75 A resolution
-, C9E261
2.3 A resolution crystal structure of the deletion construct DELTA132 reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the deletion construct as a hexamer with point group symmetry 32, similar to that of the active complex. In contrast, the UDP-alpha-D-xylose-inhibited enzyme forms a lower-symmetry, horseshoe-shaped hexameric complex. The DELTA132 and the UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces
-
alternate crystal structure of human enzyme in complex with UDP-glucose at 2.8 A resolution. The substrate-bound protein complex consists of the open homohexamer. In all subunits of the open structure, residue Thr131 has translocated into the active site occupying the volume vacated by the absent active water and partially disordered NAD+ molecule. This conformation suggests a mechanism by which the enzyme may exchange NADH for NAD+ and repolarize the catalytic water molecule bound to Asp280 while protecting the reaction intermediates
-
crystallized from a solution of 0.2 M ammonium sulfate, 0.1 M Na cacodylate, pH 6.5, and 21% PEG 8000. Diffraction data are collected to a resolution of 2.8 A. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a = 173.25, b = 191.16, c = 225.94 A and alpha = beta = gamma = 90.0
-
in mutant E161Q, the hydrolysis step becomes completely rate-limiting so that a thioester enzyme intermediate accumulates at steady state. Crystallization of mutant E161Q in the presence of 5 mM UDP-glucose and 2 mM NAD results in trapping a thiohemiacetal enzyme intermediate. Residue Cys276 is covalently modified in the structure, establishing its role as catalytic nucleophile of the reaction
-
mutant K94E, to 2.08 A resolution. Cofactor binding triggers the formation of the 32 symmetry hexamer, but substrate UDP-alpha-D-glucose is needed for the stability of the complex. Loop88-110 is the cofactor-responsive allosteric switch that drives hexamer formation, loop88-110 directly links cofactor binding to the stability of the hexamer-building interface. In the interface, loop88-110 packs against the Thr131-loop/alpha6 helix, the allosteric switch that responds to the feedback inhibitor UDP-alpha-D-xylose
-
the structure of UGDH in the crystal form reveals a hexameric arrangement, composed a trimer of dimers of six subunits
-
sitting-drop vapour-diffusion method, diffraction quality crystals (maximum dimensions of 0.1 * 0.1 * 0.1 mm) are obtained within one week at 273C using reservoir solution composed of 4.0 M NaCl, 100 mM HEPES pH 7.5. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 117.7, b = 76.7, c = 75.6 A, beta = 125.8. Crystal structure is at a resolution of 2.0 A. The overall fold is comprised of an N-terminal NAD+ dinucleotide binding domain and a C-terminal UDP-sugar binding domain connected by a long alpha-helix
-
purified recombinant wild-type and selenomethionine-labeled UgdG at 4.5 and 5.5 mg/ml, respectively, in 25 mM Tris-HCl, pH 8.3, 50 mM NaCl, 2.5 mM DTT and 1 mM NAD+, or 0.5 mM UDP-GlcA and 1 mM NAD+, 0.0005 ml of each protein and precipitant solution are mixed at 20C, 24 h, the precipitant solution contains 200 mM Li2SO4, 100 mM Tris-HCl, pH 8.5, and 30% v/v PEG 4000, or 100 mM sodium citrate, pH 5.6, 20% 2-propanol, and 20% v/v PEG 4000, vapour diffusion method, method optimization, X-ray diffraction structure determination and analysis at 2.4 A resolution for the wild-type enzyme, and at 3.4 A resolution for the SeMet-UDG
A4UTT2
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10
-
80C, 10 min, enzyme retains full activity
5.4
6.5
-
enzyme retains 93-97% of initial activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
after incubation for 1.6 h loss of 40% activity
40
-
-
rapid and irreversible inactivation above
50
-
-
without substrate, complete inactivation
80
-
-
10 min, stable
90
-
-
half-life: 10 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-mercaptoethanol stabilizes
-
UDPglucose stabilizes
-
NAD+ protects against heat inactivation
-
UDPglucose protects against heat inactivation
-
fairly stable with 2 mM dithiothreitol
-
stable during repeated freezing and thawing cycles with 10% glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-10C, little loss of activity after several weeks
-
-70C, 5 mM UDPglucose, 1 mM dithiothreitol
-
-4C, frozen in presence of UDPglucose, stable for 2 months
-
-12C, 2 weeks
-
5C, 50 mM Tris-HCl, pH 8.7, 2 mM dithiothreitol, after 24 h 90% activity left
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by nickel affinity and gel filtration; by nickel affinity and gel filtration; by nickel affinity and gel filtration
B4EB36, B4EMQ8, B4EN77
recombinant His6-tagged BceC from Escherichia coli by affinity chromatography
-
recombinant glutathione-S-transferase fusion protein
-
by nickel-NTA chromatography
-
recombinant His6-tagged UGDH from Escherichia coli by nickel affinity chromatography
-
-
Saccharum spp.
-
recombinant His6-tagged wild-type and selenomethionine-labeled UgdG from Escherichia coli BL21 and B843, respectively by affinity chromatography
A4UTT2
recombinant enzyme
Q56R95, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
Q9FM01, Q9LF33, Q9LIA8, Q9MAB5
expression of isoforms Ugd2, Ugd3, Ugd4 in Escherichia coli
-
gene Ugd(BCAL2946) cloned into the pGEM-T Easy vector, sequenced, and ligated into pET29a vector to transform Escherichia coli Top10 cells. Ugd(BCAL2946) expressed in Escherichia coli HMS 174(DE3); gene Ugd(BCAM0855) cloned into the pGEM-T Easy vector, sequenced, and ligated into pET29a vector to transform Escherichia coli Top10 cells. Ugd(BCAM0855) expressed in Escherichia coli HMS 174(DE3); gene Ugd(BCAM2034) cloned into the pGEM-T Easy vector, sequenced, and ligated into pET29a vector to transform Escherichia coli Top10 cells. Ugd(BCAM2034) expressed in Escherichia coli BL21 (DE3)
B4EB36, B4EMQ8, B4EN77
gene bceC, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
overexpression as glutathione-S-transferase fusion protein in Escherichia coli
-
expression in Escherichia coli
-
expression of mutant enzyme wild-type enzymes in Escherichia coli
-
hUGDH gene is cloned from a LNCaP cDNA library, from LNCaP C33 and C81 cells, expression of His6-tagged UGDH in Escherichia coli, expression of UGDH mutant D280N in HEK.293 cells
-
recombinant UGDH expressed in Escherichia coli
-
expression in Pichia pastoris
B5L017
expression in Escherichia coli; expression in Escherichia coli
O86422, -, Q9HY58
expressed in Escherichia coli
-
expression in Escherichia coli
-
gene ugdG, expression of His6-tagged wild-type and selenomethionine-labeled UgdG in Escherichia coli BL21 and B843, respectively
A4UTT2
genes szHasA (hyaluronan synthase gene) and szHasB (UDP-glucose-6-dehydrogenase gene) introduced into Lactococcus lactis strain NZ9000 under the control of nisA promoter and lacA promoter respectively, resulting in a dual-plasmid controlled expression system
-
overexpression in Escherichia coli JM109
-
overexpression of the enzyme from Xenopus laevis in human smooth muscle cells increases the accumulation of hyaluronan
Q56R95, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dihydrotestosterone increases UGDH expression 2.5fold in androgen-dependent cells. However, upregulation of UGDH does not affect hyaluronan synthase expression or enhance hyaluronan production
-
expression of Ugd is induced by polymyxin B through RppA, a putative response regulator of the bacterial two-component system
C3VI43, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Y10F
-, C9E261
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
-, C9E261
mutation in GXGYXG consensus motif, 2% residual activity
A222Q/S233G
-
mutation does not affect expression, stability, and secondary structure. Mutant protein is a dimer and catalytic active, with increased Km values for substrates
A222Q/S233G
-
is a dimer in solution
C276A
-
site-directed mutagenesis, strong decrease in specific activity
C276A
-
is a hexamer-dimer mixture
C276E
-
activity is not measurable at pH 8.7, 22C
C276G
-
activity is not measurable at pH 8.7, 22C
C276K
-
activity is not measurable at pH 8.7, 22C
C276L
-
activity is not measurable at pH 8.7, 22C
C276S
O60701
no enzymic activity, affinity for NAD+ similar to wild-type, retains predominantly hexameric structure
C276S
-
site-directed mutagenesis, strong decrease in specific activity
C276S
-
is a hexamer
C276Y
-
activity is not measurable at pH 8.7, 22C
D280A
-
extremely poor enzymic activity
D280E
-
site-directed mutagenesis, 3-fold increase in Km for UDP-glucose and a 2-fold reduced Vmax relative to that of the wild type
D280N
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
D280N
-
shows, exclusively, a hexameric quaternary structure in solution
D280N
-
an inactive UGDH mutant
DELTA132
-
deletion of residue Val132 from the Thr131 loop to approximate an intermediate state in the allosteric transition. The crystal structure of the deletion construct reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the construct as a hexamer with point group symmetry 32, similar to that of the active complex. The DELTA132 and UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces
E161Q
-
hydrolysis step becomes completely rate-limiting so that a thioester enzyme intermediate accumulates at steady state. Crystallization of E161Q in the presence of 5 mM UDP-glucose and 2 mM NAD results in trapping a thiohemiacetal enzyme intermediate
G13E
O60701
normal expression and stability of mutant, no enzymic activity, no photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
K220A
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K220A
-
shows, exclusively, a hexameric quaternary structure in solution
K220A
-
extremely poor enzymic activity
K220H
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K220R
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K279A
O60701
no enzymic activity, affinity for NAD+ similar to wild-type, almost exclusively found as dimer
K279A
-
site-directed mutagenesis, strong decrease in specific activity
K279A
-
is essentially a dimer
K339A
-
site-directed mutagenesis, 165fold decrease in affinity for UDP-glucose. Mutant forms a dimer, in contrast to hexameric wild-type
K339A
-
is a dimer
K94E
-
mutation in the hexamer-building interface, generates a stable enzyme dimer. 160fold decrease in kcat value
N224A
-
steady-state kinetic parameters are within an order of magnitude of the native enzyme
C260A
-
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
-
kcat-value 10fold lower than wild-type
E145Q
-
kcat-value 10fold lower than wild-type
T118A
-
160fold reduction of kcat value
additional information
-
differences in host colonization between wild-type and UDPDH mutant
additional information
-
comparison of sequence homologies with bacterial enzymes
additional information
B4EB36, B4EMQ8, B4EN77
inactivation of gene Ugd(BCAL2946) results in increased sensitivity to polymyxin B and this sensitivity can be overcome when either genes Ugd(BCAL2946) or Ugd(BCAM0855) but not gene ugd(BCAM2034) is expressed from plasmids. Growth of a conditional Ugd(BCAL2946) mutant, created in the DELTAUgd(BCAM0855) background, is significantly impaired under non-permissive conditions. Growth can be rescued by either Ugd(BCAL2946) or Ugd(BCAM0855) expressed in trans, but not by Ugd(BCAM2034); inactivation of gene Ugd(BCAL2946) results in increased sensitivity to polymyxin B and this sensitivity can be overcome when either genes Ugd(BCAL2946) or Ugd(BCAM0855) but not gene ugd(BCAM2034) is expressed from plasmids. Growth of a conditional Ugd(BCAL2946) mutant, created in the DELTAUgd(BCAM0855) background, is significantly impaired under non-permissive conditions. Growth can be rescued by either Ugd(BCAL2946) or Ugd(BCAM0855) expressed in trans, but not by Ugd(BCAM2034); inactivation of gene Ugd(BCAL2946) results in increased sensitivity to polymyxin B and this sensitivity can be overcome when either genes Ugd(BCAL2946) or Ugd(BCAM0855) but not gene ugd(BCAM2034) is expressed from plasmids. Growth of a conditional Ugd(BCAL2946) mutant, created in the DELTAUgd(BCAM0855) background, is significantly impaired under non-permissive conditions. Growth can be rescued by either Ugd(BCAL2946) or Ugd(BCAM0855) expressed in trans, but not by Ugd(BCAM2034)
Y10S
-, C9E261
mutation in GXGYXG consensus motif, 3% residual activity
additional information
-
overexpression of enzyme plus transformation of gene cluster for K5 polysaccharide production, 15fold increase in enzyme activity, decrease in K5 polysaccharide formation
K94E
-
substitution prevents hexamer formation. Mutant does not display hysteresis
additional information
-
perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the hUGDH structure, thereby changing the motional fluctuation pattern at the oligomeric interfaces. A large-magnitude cooperative motion at the oligomeric interfaces is a critical factor in interfering with the hexamer formation of the enzyme. Structural stability at the dimeric interface is necessary to retain the hexameric structure of UGDH
additional information
-
UGDH overexpression stimulates hyaluronan production in HEK293 cells
T131S
-
steady-state kinetic parameters are within an order of magnitude of the native enzyme
additional information
C3VI43, -
construction by Tn5 transposon mutagenesis of a knockout mutant of ugd, that is extremely sensitive to polymyxin B, presumably because of alterations in lipopolysaccharide structure and cell surface architecture in the mutant. The mutant is defective in swarming, expresses lower levels of virulence factor hemolysin, and has lower cell invasion ability. Complementation of the ugd or galU mutant with the full-length ugd gene leads to the restoration of wild-type phenotypic traits, phenotype, overview
additional information
O86422, -, Q9HY58
mutant lacking PA2022 activity and double mutant lacking PA2022 and isoform PA3559 activity are more susceptible to chloramphenicol, ceffotaxime, and ampicillin; mutant lacking PA3559 activity shows reduced resistance to polymyxin B
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
possibility that gallic acid and quercetin may modulate human breast cancer cell proliferation by inhibiting UGDH
medicine
-
UGDH content in prostatic acini is a novel candidate biomarker that may complement the development of a multi-biomarker panel for detecting prostate cancer within the tumor adjacent field on a histologically normal biopsy specimen
agriculture
L0N5L6
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
pharmacology
-
target for inhibitor design