5.1.3.2: UDP-glucose 4-epimerase
This is an abbreviated version!
For detailed information about UDP-glucose 4-epimerase, go to the full flat file.
Word Map on EC 5.1.3.2
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5.1.3.2
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polysaccharide
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galactokinase
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leloir
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galactosemia
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galactose-1-phosphate
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udp-galnac
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udp-n-acetylglucosamine
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galactose-inducible
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kluyveromyces
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pyrophosphorylase
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fragilis
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uridylyltransferase
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udp-n-acetylgalactosamine
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udpglucose
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udp-sugars
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galnac
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mutarotase
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galactose-containing
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o-antigens
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udp-glucuronic
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medicine
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synthesis
- 5.1.3.2
- polysaccharide
- galactokinase
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leloir
- galactosemia
- galactose-1-phosphate
- udp-galnac
- udp-n-acetylglucosamine
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galactose-inducible
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kluyveromyces
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pyrophosphorylase
- fragilis
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uridylyltransferase
- udp-n-acetylgalactosamine
- udpglucose
- udp-sugars
- galnac
- mutarotase
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galactose-containing
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o-antigens
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udp-glucuronic
- medicine
- synthesis
Reaction
Synonyms
4-Epimerase, 6xHis-rGalE, ABD1_580, An14g03820, AtUGE1, AtUGE2, AtUGE3, AtUGE4, AtUGE5, CaGAL10, CapD, epimerase Ab-WbjB, Epimerase, uridine diphosphoglucose, fnlA, GAL10, Gal10p, Galactowaldenase, GalE, galE-1, galE-2, galE1, GalESp1, GalESp2, GNE, GNE2, H3634, HvUGE1, HvUGE2, HvUGE3, MdUGE1, More, OsUGE-1, OsUGE1, PsUGE1, Rdh1, rGalE, Rv3634c, TbGalE, TM0509, TMGalE, UDP-D-galactose 4-epimerase, UDP-D-glucose/UDP-D-galactose 4-epimerase, UDP-Gal 4-epimerase, UDP-Gal/Glc 4-epimerase, UDP-galactose 4'-epimerase, UDP-galactose 4-epimerase, UDP-galactose-4'-epimerase, UDP-galactose-4-epimerase, UDP-Glc 4-epimerase, UDP-Glc(NAc) 4-epimerase, UDP-GlcNAc 4-epimerase, UDP-GlcNAc/Glc 4-epimerase, UDP-glucose 4'-epimerase, UDP-glucose 4-epimerase, UDP-glucose 4-epimerase 1, UDP-glucose 4-epimerase 4, UDP-glucose epimerase, UDP-glucose-4-epimerase, UDP-glucose/-galactose 4-epimerase, UDP-hexose 4-epimerase, UDP-N-acetyl-glucosamine 4,6-dehydratase, UDP-sugar 4-epimerase, UDP-Xyl 4-epimerase, UDP-xylose 4-epimerase, UDPG-4-epimerase, UDPgalactose 4-epimerase, UGE, UGE-1, UGE1, UGE1:GUS, Uge1p, UGE2, UGE3, UGE3:GUS, UGE4, UGE5, UgeA, Uridine diphosphate galactose 4-epimerase, Uridine diphosphate glucose 4-epimerase, uridine diphosphate-galactose-4'-epimerase, Uridine diphospho-galactose-4-epimerase, Uridine diphosphogalactose-4-epimerase, Uridine diphosphoglucose 4-epimerase, Uridine diphosphoglucose epimerase, uridine-diphospho-glucose 4-epimerase, WbjB
ECTree
5.1.3.2 UDP-glucose 4-epimeraseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 5.1.3.2 - UDP-glucose 4-epimerase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1,2-Cyclohexanedione
Saccharomyces fragilis
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protection by substrates and competitive inhibitors
2',3'-O-(2,4,6-Trinitrocyclohexadienylidene)uridine 5'-monophosphate
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powerful reversible inhibitor
2-Hydroxy-5-nitrobenzyl bromide
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a combination of NAD+ and UDP protects against modification
5,5'-dithiobis(2-nitrobenzoate)
Saccharomyces fragilis
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reactivation in presence of mercaptoethanol, protection by UDPglucose or UDPgalactose, inactivated enzyme retains the dimeric structure and NAD+ is not dissociated from the protein moiety
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
fructose 1,6-diphosphate
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inhibition is enhanced by combination with UMP
Galactose plus UMP
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strong inhibition in the presence of UMP, no inhibition by UMP or sugar alone
L-Xylose plus UMP or UDP
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inactivation due to reduction of the epimerase NAD+
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PCMB
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dissociates the native epimerase into inactive mercurated monomers, reconstitution of the functional holoenzyme is done by reduction with dithiothreitol and addition of extra NAD+, reactivation is most effective at pH 8.1
Sodium cyanoborohydride
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NAD+ associated with the wild type enzyme is subject to UMP-dependent reduction, mutant proteins K153M and K153A bind UMP very well, but the rate at which NAD+ associated with them is reduced by sodium cyanoborohydride is almost insensitive to the presence of UMP
UDP-6-deoxygalactose
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weak competitive inhibitor with respect to UDPgalactose
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
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powerful competitive
5'-UMP
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the native enzyme is completely insensitive to inhibition, the desensitized enzyme is strongly inhibited. Desensitization by heat converts the enzyme to its ultimate catalytic form
5'-UMP
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string competitive inhibitor. The enzyme contains 0.77 mol of 5'-UMP per dimer
5'-UMP
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a competitive, irreversible inhibitor, binds per dimer of epimerase as isolate and causes inactivation, transition profiles indicate the existence of a stable intermediate with one inhibitor-binding site remaining unoccupied. Reductive inhibition of this intermediate reduces the activity to 58% with modification of one catalytic site, negative cooperativity, inhibition mechanism, overview. Protective effect of 5'-UMP against modification of the arginine located at the catalytic site by 1,2-cyclohexanedione
5'-UMP
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epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
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diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
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diethyldicarbonate
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almost complete inhibition at 5 mM after 30 min incubation
diethyldicarbonate
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reversal of inhibition by hydroxylamine. Modification of 1 essential histidine residue is responsible for loss in catalytic activity
galactose 6-phosphate
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activation of the minor enzyme form; partial inhibition of major enzyme form
glucose 1-phosphate
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partial inhibition of minor enzyme form, no effect on major enzyme form
glucose 1-phosphate
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partial inhibition of minor enzyme form, no effect on major enzyme form
glucose plus UMP
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strong inhibition in the presence of UMP, no inhibition by UMP or sugar alone
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glucose plus UMP
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NAD+ associated with the wild type enzyme is subject to UMP-dependent reduction by sugars such as glucose and arabinose, but the mutant proteins K153M and K153A are not reduced by sugars in the presence or absence of UMP
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L-arabinose
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on treatment with L-arabinose, 2 mM, in presence of UMP, 0.5 mM, both the native enzyme and the reconstituted enzyme are inactivated at an indistinguishable rate of inactivation
L-arabinose
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epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
L-Arabinose plus UMP or UDP
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NAD+ associated with the wild type enzyme is subject to UMP-dependent reduction by sugars such as glucose and arabinose, but the mutant proteins K153M and K153A are not reduced by sugars in the presence or absence of UMP
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L-Arabinose plus UMP or UDP
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inactivation due to reduction of the epimerase NAD+
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NADH
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NADH associated with the purified enzyme is a component of the inactive, abortive complexes, enzyme-NADH-uridine nucleotide, that contain tightly bound uridine nucleotides in place of the epimerization intermediate UDP-4-keto-alpha-D-hexoglucopyranose. These complexes are produced in vivo in the course of bacterial growth
p-chloromercuribenzoate
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no inactivation by p-chloromercuribenzoate
additional information
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inhibited by combination of 100 microM NADH and 10 microM NAD+
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additional information
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no inactivation by the UDP-D-fucose or D-fucose alone or by UDP-D-fucose plus 5'-UMP
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additional information
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NAD+ associated with the wild type enzyme is also subject to UMP-dependent reduction by sodium cyanoborohydride. The mutant protein binds UMP very well, but the rate at which NAD+ associated with them is reduced by sodium cyanoborohydride is almost insensitive to the presence of UMP. The purified wild type enzyme contains significant amounts of NADH bound to the coenzyme site, however the purified mutants K153M and K153A contain very little NADH
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