Information on EC 5.1.3.2 - UDP-glucose 4-epimerase

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

EC NUMBER
COMMENTARY hide
5.1.3.2
-
RECOMMENDED NAME
GeneOntology No.
UDP-glucose 4-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose = UDP-alpha-D-galactose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
additional information
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
colanic acid building blocks biosynthesis
-
-
D-galactose degradation I (Leloir pathway)
-
-
D-galactose degradation III
-
-
D-galactose degradation V (Leloir pathway)
-
-
degradation of hexoses
-
-
Galactose metabolism
-
-
Metabolic pathways
-
-
mycolyl-arabinogalactan-peptidoglycan complex biosynthesis
-
-
stachyose degradation
-
-
superpathway of UDP-glucose-derived O-antigen building blocks biosynthesis
-
-
UDP-D-galactose biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-89-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes uge3 and uge5 encoding isozymes Uge3 and Uge5
-
-
Manually annotated by BRENDA team
genes uge3 and uge5 encoding isozymes Uge3 and Uge5
-
-
Manually annotated by BRENDA team
gene BAS5114
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
NCTC 11168
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
enzyme exists in two distinct forms
-
-
Manually annotated by BRENDA team
O86:B7
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Homo sapiens CHO-K1
CHO-K1
-
-
Manually annotated by BRENDA team
L.
-
-
Manually annotated by BRENDA team
CL 87
-
-
Manually annotated by BRENDA team
CL 87
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. pyramidalis
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Saccharomyces fragilis
-
-
-
Manually annotated by BRENDA team
gene uge1; strain ARC039, gene uge1
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strains YT-1 and NTU103, gene galE
-
-
Manually annotated by BRENDA team
; strains HB8 and HB27, gene galE
-
-
Manually annotated by BRENDA team
Torulopsis candida
-
-
-
Manually annotated by BRENDA team
Trigonella sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pv.campestris, gene galE
UniProt
Manually annotated by BRENDA team
pv.campestris, gene galE
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-D-glucose
?
show the reaction diagram
-
-
-
-
-
CDP-D-glucose
?
show the reaction diagram
-
-
-
-
-
D-fructose
D-tagatose
show the reaction diagram
B1X789
-
-
-
?
D-galactose
D-glucose
show the reaction diagram
B1X789
the catalytic efficiencies of GalE for D-galactose is much lower than for UDP-galactose
-
-
?
D-glucose
D-galactose
show the reaction diagram
B1X789
-
-
-
?
D-psicose
D-sorbose
show the reaction diagram
B1X789
-
-
-
?
D-sorbose
D-psicose
show the reaction diagram
B1X789
-
-
-
?
D-tagatose
D-fructose
show the reaction diagram
B1X789
the catalytic efficiencies of GalE for D-tagatose is much lower than for UDP-galactose
-
-
?
Deoxy-UDP-D-glucose
?
show the reaction diagram
-
-
-
-
-
TDP-6-deoxy-D-galactose
?
show the reaction diagram
-
-
-
-
-
TDP-D-glucose
TDP-D-galactose
show the reaction diagram
UDP-6-deoxy-D-glucose
?
show the reaction diagram
-
-
-
-
-
UDP-6-deoxygalactose
UDP-6-deoxyglucose
show the reaction diagram
-
-
-
-
UDP-alpha-D-galactose
UDP-alpha-D-glucose
show the reaction diagram
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
UDP-D-fucose
?
show the reaction diagram
-
-
-
-
-
UDP-D-galactose-hexodialose
?
show the reaction diagram
-
-
-
-
-
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
UDP-D-xylose
?
show the reaction diagram
-
-
-
-
-
UDP-D-xylose
UDP-L-arabinose
show the reaction diagram
UDP-galactose
UDP-glucose
show the reaction diagram
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
UDP-Glc
UDP-Gal
show the reaction diagram
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
UDP-L-arabinose
?
show the reaction diagram
-
-
-
-
-
UDP-L-arabinose
UDP-D-xylose
show the reaction diagram
the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
-
?
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
UDP-D-glucose
UDP-D-galactose
show the reaction diagram
UDP-D-xylose
UDP-L-arabinose
show the reaction diagram
B0M3E8
-
-
-
r
UDP-galactose
UDP-glucose
show the reaction diagram
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
UDP-Glc
UDP-Gal
show the reaction diagram
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
the amino acids that interact with NADH are Asp31, Asn35, Ser36, Lys83, Asn98, Tyr147, and Lys151
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
enzyme activity is 28.6 U/mg protein at a metal concentration of 1 mM
Ba2+
enzyme activity is 54.6 U/mg protein at a metal concentration of 1 mM
Ca2+
enzyme activity is 47.8 U/mg protein at a metal concentration of 1 mM
Co2+
enzyme activity is 44.7 U/mg protein at a metal concentration of 1 mM
Cu2+
enzyme activity is 21.8 U/mg protein at a metal concentration of 1 mM
Fe3+
enzyme activity is 20.3 U/mg protein at a metal concentration of 1 mM
Hg2+
1 mM Hg2+ abolishes enzyme function entirely
Li+
enzyme activity is 43.7 U/mg protein at a metal concentration of 1 mM
MgCl2
-
is included in assay medium
NaCl
-
increases the activity
Zn2+
enzyme activity is 17.2 U/mg protein at a metal concentration of 1 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-Cyclohexanedione
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
2',3'-O-(2,4,6-Trinitrocyclohexadienylidene)uridine 5'-monophosphate
-
powerful reversible inhibitor
2,3-Butanedione
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
2-Hydroxy-5-nitrobenzyl bromide
-
a combination of NAD+ and UDP protects against modification
5,5'-dithiobis(2-nitrobenzoate)
Saccharomyces fragilis
-
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
5-(adenosine-5'-diphosphoryl)-D-ribose
-
reductive inhibition
5-(thymidine-5'-diphosphoryl)-D-glucose
-
reductive inhibition
5-(Thymidine-5'-diphosphoryl)-D-ribose
-
reductive inhibition
bisprasin
-
-
Cu2+
5 mM, 95% loss of activity
D-galactose
Torulopsis candida
-
-
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
diethyldicarbonate
diethylstilbestrol
Dimethylsulfoxide
10%, 26% inhibition
ebselen
Ethacrynic acid
fructose 1,6-diphosphate
-
inhibition is enhanced by combination with UMP
galactose 6-phosphate
Galactose plus UMP
-
strong inhibition in the presence of UMP, no inhibition by UMP or sugar alone
-
glucose 1-phosphate
Glucose plus UMP
haloprogin
Hg2+
complete inhibition, recombinan t enzyme
L-arabinose
L-Arabinose plus UMP or UDP
L-Xylose plus UMP or UDP
-
inactivation due to reduction of the epimerase NAD+
-
methanol
10%, 26% inhibition
NaBH4
-
reductive inhibition
NADPH
-
very weak inhibitory effect
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
-
P1-5'-Uridine-P2-glucose-6-yl diphosphate
-
-
PCMB
-
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
Phenylglyoxal
Saccharomyces fragilis
-
protection by substrates and competitive inhibitors
psammaplin A
Salt
-
moderately inhibited by high salt concentrations
Showdomycin
-
-
Sodium cyanoborohydride
-
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
Thymidine diphospho-6-deoxy-D-xylo-4-hexosulose
-
reductive inhibition
-
UDP-6-deoxygalactose
-
weak competitive inhibitor with respect to UDPgalactose
UDP-N-acetylgalactosamine
-
competitive, binding study
UDP-N-acetylglucosamine
-
competitive, binding study
Uridine 5'-diphosphate bromoacetol
-
-
Uridine 5'-diphosphate chloroacetol
-
-
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
powerful competitive
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fructose 4-phosphate
-
stimulates
fructose 6-phosphate
-
stimulates
Galactose 1-phosphate
galactose 6-phosphate
glucose 1-phosphate
-
stimulates
glucose 6-phosphate
NAD+
non-covalently bound, released from the enzyme after denaturation with aqueous ethanol. Each enzyme molecule contains one molecule of NAD+
UDP
-
activates the reduction of epimerase-bound NAD+
UMP
-
activates the reduction of epimerase-bound NAD+
additional information
-
does not require external NAD+ for activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26.4
D-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
2 - 37
D-tagatose
B1X789
in McIlvaine buffer (pH 7.5), at 35C
0.23
UDP-alpha-D-galactose
pH 6.5, 60C
0.06 - 260
UDP-alpha-D-glucose
0.057 - 0.29
UDP-D-galactose
0.31
UDP-D-glucose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.15
UDP-D-xylose
pH 8.6, 25C
0.04 - 0.295
UDP-Gal
0.035 - 3.9
UDP-galactose
0.16 - 1.07
UDP-GalNAc
0.055 - 0.37
UDP-Glc
0.2 - 1.087
UDP-GlcNAc
0.055 - 1.2
UDP-glucose
0.16
UDP-L-arabinose
pH 8.6, 25C
0.146 - 0.437
UDP-N-acetyl-alpha-D-glucosamine
0.15
UDP-xylose
pH 8.6, 25C
0.0083 - 1.67
UDPgalactose
0.25 - 1.4
UDPglucose
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00026
D-galactose
Escherichia coli
B1X789
in McIlvaine buffer (pH 7.5), at 35C
0.00545
D-tagatose
Escherichia coli
B1X789
in McIlvaine buffer (pH 7.5), at 35C
1
UDP-alpha-D-galactose
Pyrococcus horikoshii
O73960
pH 6.5, 60C
0.073 - 760
UDP-alpha-D-glucose
9 - 64
UDP-D-galactose
17
UDP-D-xylose
Pisum sativum
B0M3E8
pH 8.6, 25C
0.046 - 750
UDP-galactose
0.12 - 247.9
UDP-GalNAc
0.07 - 82.3
UDP-GlcNAc
2 - 73.95
UDP-glucose
23
UDP-L-arabinose
Pisum sativum
B0M3E8
pH 8.6, 25C
0.37 - 2.62
UDP-N-acetyl-alpha-D-glucosamine
17
UDP-xylose
Pisum sativum
B0M3E8
pH 8.6, 25C
0.073 - 960
UDPgalactose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000097
D-galactose
Escherichia coli
B1X789
in McIlvaine buffer (pH 7.5), at 35C
71
0.000023
D-tagatose
Escherichia coli
B1X789
in McIlvaine buffer (pH 7.5), at 35C
2197
4.34
UDP-alpha-D-galactose
Pyrococcus horikoshii
O73960
pH 6.5, 60C
891
0.49 - 3400
UDP-alpha-D-glucose
103 - 578
UDP-D-galactose
115
UDP-D-xylose
Pisum sativum
B0M3E8
pH 8.6, 25C
341
0.78 - 3333
UDP-galactose
28
UDP-glucose
Pisum sativum
B0M3E8
pH 8.6, 25C
64
141
UDP-L-arabinose
Pisum sativum
B0M3E8
pH 8.6, 25C
5226
1.55 - 6.61
UDP-N-acetyl-alpha-D-glucosamine
115
UDP-xylose
Pisum sativum
B0M3E8
pH 8.6, 25C
1013
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
5'-UMP
-
25C, pH 8.8
0.036
UDP
; 25C, pH 8.0
0.032
UMP
; 25C, pH 8.0
0.2
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
pH 8.8
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
bisprasin
Trypanosoma brucei
-
-
5.6 - 12
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
17 - 75
diethylstilbestrol
0.014 - 0.62
ebselen
3.1 - 14
Ethacrynic acid
0.5 - 13
haloprogin
3.6 - 15
psammaplin A
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.6
-
GALE activity evaluated in samples by monitoring the conversion of UDP-gal to UDP-glc. Assays stopped by the addition of 237.5 microliter of ice-cold water followed immediately by filtration through 0.2-micrometer nylon micro-spin columns (Corning) to remove proteins and particulates before high performance liquid chromatography analysis.
1.7
native protein, substrate is UDP-glucose; purified native enzyme, substrate UDP-Glc
4.6
purified recombinant detagged enzyme, substrate UDP-Glc; recombinant Pisum protein, substrate is UDP-glucose
6.67
purified native enzyme, substrate UDP-D-Xyl
6.7
purified native enzyme, substrate UDP-L-Ara
7.9
-
-
16.7
specific activity of recombinant enzyme in cell lysate after expression in Escherichia coli
19.8
native protein, substrate is UDP-galactose; purified native enzyme, substrate UDP-Gal
21.1
purified recombinant detagged enzyme, substrate UDP-L-Ara
38.9
purified recombinant detagged enzyme, substrate UDP-D-Xyl; specific activity of recombinant enzyme after purification by a DEAE-sepharose FF column
49
specific activity of recombinant enzyme after purification by a Ni-sepharose colum
53.3
purified recombinant detagged enzyme, substrate UDP-Gal; recombinant Pisum protein, substrate is UDP-galactose
66
-
liver
210
-
mammary
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.3
-
activity of the wild-type enzyme is pH-independent in the pH-range of 5.5-9.3
7.5
B1X789
-
8 - 9.5
; interconversion of UDP-glucose and UDP-galactose
8.5
-
assay at
8.5 - 9
recombinant enzyme
8.5
Trigonella sp.
-
-
8.9
-
assay at
9
-
; recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
-
MES buffer
6 - 10.5
-
about 65% of maximal activity at pH 6 and 10.5
6.4 - 9.6
-
6.4: 68% loss of maximal activity, 9.6: 79% of maximal activity
6.5 - 9.5
-
Tris/HCl buffer
6.6 - 9.2
-
about 50% of maximal activity at pH 6.6 and 9.2
6.7 - 8.1
-
6.7: 91% of maximal activity, 8.1: 88% of maximal activity
7 - 9.7
-
7: about 50% of maximal activity, 9.7: about 40% of maximal activity
7.6 - 9.5
-
7.6: about 25% of maximal activity, 9.5: maximal activity
8.5 - 9
maximum activity of recombinant PsUGE1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
maximum activity of recombinant PsUGE1; recombinant enzyme
50
-
; recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
834
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
levels of HvUGE1 mRNA are low in day 1 and day 3 coleoptiles, increases approximately 28fold in day 5 coleoptiles
Manually annotated by BRENDA team
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
Manually annotated by BRENDA team
-
skin
Manually annotated by BRENDA team
-
during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
Manually annotated by BRENDA team
expression of HvUGE1 is highest in leaf tips, rapidly decreases to very low levels in the basal region of the leaves
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Brucella abortus (strain 2308)
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
Burkholderia pseudomallei (strain 1710b)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)