1.1.1.22: UDP-glucose 6-dehydrogenase
This is an abbreviated version!
For detailed information about UDP-glucose 6-dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.22
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1.1.1.22
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udp-glucuronic
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polysaccharide
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ugdhs
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glycosaminoglycans
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hyaluronan
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pyrophosphorylase
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udp-xylose
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glucuronic
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glucuronidation
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udp-glca
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exopolysaccharide
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udp-sugars
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medicine
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glca
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udpga
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udp-d-glucuronate
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udp-glucuronyltransferase
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hasas
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pharmacology
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agriculture
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molecular biology
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synthesis
- 1.1.1.22
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udp-glucuronic
- polysaccharide
-
ugdhs
- glycosaminoglycans
- hyaluronan
-
pyrophosphorylase
- udp-xylose
-
glucuronic
-
glucuronidation
- udp-glca
- exopolysaccharide
- udp-sugars
- medicine
-
glca
-
udpga
- udp-d-glucuronate
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udp-glucuronyltransferase
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hasas
- pharmacology
- agriculture
- molecular biology
- synthesis
Reaction
Synonyms
ADH-like UDP-glucose dehydrogenase, AglM, BceC, Cj1441c, dehydrogenase, uridine diphosphoglucose, dual specificity UDP-glucose dehydrogenase, GbUGD, GH_D12G1806, HasB, HasB2, HVO_1531, jekyll m151, kfiD, PA2022, PA3559, PH02Gene21682, sqv-4, Sugarless protein, UDG1, UDP-alpha-D-glucose:NAD oxidoreductase, UDP-D-glucose dehydrogenase, UDP-GDH, UDP-Glc dehydrogenase, UDP-Glc DH, UDP-GlcDH, UDP-GlcDHase, UDP-glucose dehydrogenase, UDPDH, UDPG dehydrogenase, UDPG-DH, UDPG:NAD oxidoreductase, UDPGD, UDPGDH, UDPGDH-A, UDPGDH-B, UDPGlc dehydrogenase, UDPglucose dehydrogenase, UDPglucose:NAD+ oxidoreductase, Ugd, UGD1, Ugd2, UgdG, UGDH, UGDH4, 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, uridyl phosphate dehydrogenase, VNG1048G, VNG_1048G
ECTree
1.1.1.22 UDP-glucose 6-dehydrogenaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 1.1.1.22 - UDP-glucose 6-dehydrogenase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
gallic acid
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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+
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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
phycocyanin
mixed-type inhibitor with respect to both UDP-glucose and NAD+
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phycocyanobilin
competitive with respect to UDP-glucose and non-competitive with respect to NAD+. Phycocyanobilin is also effective in reducing the colony formation capacity of PC-3 prostate cancer cells and FTC-133 thyroid cancer cells
quercetin
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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
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alkylates a thiol group of cysteine in the catalytic centre via being specifically bound instead of the substrate
NADH
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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
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stronger inhibition with intestinal cell enzyme than with rat liver enzyme
piperine
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non-competitive, reversible, non-pH-dependent, 90% inhibition at concentration 0.05 mM and 10% inhibition at concentration 0.01 mM
UDP-xylose
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allosteric feedback inhibitor, reduces significantly the activity of the enzyme
Zn2+
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the presence of Zn2+ ions markedly stimulates catalytic activity
additional information
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enzyme is active in the absence of metal ions
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additional information
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the enzyme from serotype K30 is not inhibited by NAD+, in contrast to Escherichia coli K-12
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additional information
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no substrate inhibition, K+ is not inhibitory up to 500 mM, not inhibitory: dimethyldicarbonate, EDTA
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additional information
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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
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additional information
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inhibition of human UDP-glucose dehydrogenase expression using siRNA expression vector in breast cancer cells
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