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Information on EC 5.1.3.2 - UDP-glucose 4-epimerase
for references in articles please use BRENDA:EC5.1.3.2
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EC Tree 5 Isomerases
5.1 Racemases and epimerases
5.1.3 Acting on carbohydrates and derivatives
5.1.3.2 UDP-glucose 4-epimerase
IUBMB Comments
Requires NAD+. Also acts on UDP-2-deoxyglucose.
The enzyme appears in viruses and cellular organisms
- 5.1.3.2
- polysaccharide
- galactokinase
-
leloir
- galactosemia
- galactose-1-phosphate
- udp-galnac
- udp-n-acetylglucosamine
-
galactose-inducible
-
kluyveromyces
-
pyrophosphorylase
- fragilis
-
uridylyltransferase
- udp-n-acetylgalactosamine
- udpglucose
- udp-sugars
- galnac
- mutarotase
-
galactose-containing
-
o-antigens
-
udp-glucuronic
- medicine
- synthesis
showSynonyms
gal10, udp-galactose 4-epimerase, 4-epimerase, udp-glucose 4-epimerase, udp-galactose-4-epimerase, udp-galactose 4'-epimerase, udp-glucose 4'-epimerase, udp-glucose-4-epimerase, udp-glucose epimerase, gal10p, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-Epimerase
-
-
-
-
A6180
ABD1_580
AglW
4-epimerase with broad specificity towards UDP-sugars, cf. EC 5.1.3.7
An14g03820
Cj1131c
epimerase Ab-WbjB
Epimerase, uridine diphosphoglucose
-
-
-
-
fnlA
GAL10
Gal10p
Galactowaldenase
GalE
galE-1
galE-2
galE1
GalESp1
GalESp2
GNE
H3634
HvUGE1
HvUGE2
KfoA
Rv3634c
TM0509
TMGalE
UDP-D-galactose 4-epimerase
-
-
-
-
UDP-Gal 4-epimerase
UDP-Gal/Glc 4-epimerase
UDP-galactose 4'-epimerase
UDP-galactose 4-epimerase
UDP-galactose epimerase
UDP-galactose-4'-epimerase
UDP-galactose-4-epimerase
UDP-galactose/glucose-4-epimerase
UDP-Glc 4-epimerase
UDP-GlcNAc/Glc 4-epimerase
UDP-glucose 4-epimerase
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
UDPG-4-epimerase
-
-
-
-
UDPgalactose 4-epimerase
-
-
-
-
UGE
UGE1
Uge1p
UGE2
UGE3
UGE4
UGE5
UgeA
Uridine diphosphate galactose 4-epimerase
Uridine diphosphate glucose 4-epimerase
-
-
-
-
uridine diphosphate-galactose-4'-epimerase
uridine diphosphate-galactose/glucose-4-epimerase
Uridine diphospho-galactose-4-epimerase
-
-
-
-
Uridine diphosphoglucose 4-epimerase
-
-
-
-
Uridine diphosphoglucose epimerase
-
-
-
-
Uxe
WbjB
additional information
Gal10p
-
the first and the last enzyme of the Leloir pathway, galactose mutarotase and UDP-galactose 4-epimerase, are comtained within a single polypeptide chain referred to as Gal10p
Galactowaldenase
-
-
-
-
UDP-galactose 4-epimerase
-
-
-
-
Uridine diphosphate galactose 4-epimerase
-
-
-
-
Uridine diphosphate galactose 4-epimerase
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose = UDP-alpha-D-galactose
a nucleoside diphospho-4-ulose of the configuration D-xylo-4-hexosulose is an intermediate in the reaction
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
presence of at least one essential Arg at the substrate-binding region of the active site
-
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
Ser124 and Tyr149 are likely to play important roles in the catalytic mechanism
-
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
-
-
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
structurereactivity studies and reaction mode, acid-base catalysis of hydride transfer, overview
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
revolving door reaction mechanism, Tyr149 is the base catalyst for hydride transfer, overview. The enzyme undergoes a conformational change upon binding of the UDP sugar, which is in fact a result of the binding of the UMP-moiety of the substrate. The conserved lysine from the YxxxK motif plays an important role in the activation of the cofactor, as due to the conformational change, the 6-ammonium group is hydrogen-bonded to both the 2'- and 3'-hydroxylgroups of the nicotinamide riboside of NAD+
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
-
-
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
additional information
epimerization
-
-
specificity for carbon 4, forming a 4-hexosulose intermediate
-
epimerization
-
of uridine diphosphate (UDP)-glucose to a galactose derivated UDP-galactose
epimerization
-
The reaction mechanism of UGE is thought to occur via transfer of the 4'-OH hydrogen of the sugar to the nicotinamide ring of noncovalently bound NAD+, rotation of the resulting 4'-ketopyranose intermediate in the active site, and transfer of the hydride from the nicotinamide ring of NADH back to C-4 of the sugar.
additional information
-
catalyses the interconversion of UDP-Gal and UDPGlc
additional information
catalyses the interconversion of UDP-Gal and UDPGlc
additional information
-
HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
additional information
HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
additional information
-
HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance.
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
colanic acid building blocks biosynthesis, D-galactose degradation I (Leloir pathway), D-galactose detoxification, mycolyl-arabinogalactan-peptidoglycan complex biosynthesis, stachyose degradation, superpathway of UDP-glucose-derived O-antigen building blocks biosynthesis, UDP-alpha-D-galactose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
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CAS REGISTRY NUMBER
COMMENTARY
9032-89-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-galactose
D-glucose
Substrates: the catalytic efficiencies of GalE for D-galactose is much lower than for UDP-galactose
Products: -
Products: -
?
D-tagatose
D-fructose
Substrates: the catalytic efficiencies of GalE for D-tagatose is much lower than for UDP-galactose
Products: -
Products: -
?
UDP-L-arabinose
UDP-D-xylose
Substrates: the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
Products: -
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r
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-alpha-D-glucosamine
Substrates: epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose
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r
UDP-N-acetylgalactosamine
UDP-N-acetylglucosamine
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
XP_020276977.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
XP_006477432.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
CCQ00728.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
CCQ00728.1
Substrates: cf. EC 5.1.3.7
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
CCQ00728.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: the enzyme (AglW) is a 4-epimerase with broad specificity towards UDP-sugars, cf. EC 5.1.3.7
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
XP_026409344.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: the enzyme preferentially catalyzes the conversion between UDP-GlcNAc and UDPGalNAc above UDP-Glc and UDP-Gal, cf. EC 5.1.3.7
Products: -
Products: -
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: the enzyme preferentially catalyzes the conversion between UDP-GlcNAc and UDPGalNAc above UDP-Glc and UDP-Gal. 15% and 40% of UDP-Glc and UDP-Gal, respectively, are converted at equilibrium. cf. EC 5.1.3.7
Products: -
Products: -
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
XP_020276977.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: the NAD+-dependent enzyme is responsible for reversibly inverting the 4-hydroxyl configuration of UDP-alpha-D-galactose to form UDP-alpha-D-glucose
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: via 4-ketose intermediate
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: via 4-ketose intermediate, UDP-glucose is bound within the active site cleft, substrate binding structure, overview
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Q81JK4, Q81K34
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
XP_006477432.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: with NAD+ as cofactor, UDP-4-ketopyranose and NADH are reaction intermediates. Weak binding of the 4-ketopyranosyl moiety and strong binding of the UDP-moiety within a substrate domain allow either face of the 4-ketopyranosyl moiety to accept hydride from NADH, pH-dependent charge transfer complex between Tyr149 and NAD+
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
CCQ00728.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
CCQ00728.1
Substrates: KfoA shows a strong preference for acetylated substrates in vitro, cf. EC 5.1.3.7
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
CCQ00728.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
CCQ00728.1
Substrates: KfoA shows a strong preference for acetylated substrates in vitro, cf. EC 5.1.3.7
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: reaction mechanism modelling, overview
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: anthocyanin biosynthesis
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: the enzyme (AglW) is a 4-epimerase with broad specificity towards UDP-sugars, cf. EC 5.1.3.7
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
XP_026409344.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: the enzyme preferentially catalyzes the conversion between UDP-GlcNAc and UDPGalNAc above UDP-Glc and UDP-Gal, cf. EC 5.1.3.7
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: the enzyme preferentially catalyzes the conversion between UDP-GlcNAc and UDPGalNAc above UDP-Glc and UDP-Gal. 15% and 40% of UDP-Glc and UDP-Gal, respectively, are converted at equilibrium. cf. EC 5.1.3.7
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: Leloir pathway of membrane polysaccharide synthesis
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
Substrates: epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: Galactose metabolism is essential for the survival of Trypanosoma brucei, the etiological agent of African sleeping sickness.
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?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: residues Ser123, Tyr147, Asn177, Asn197, Arg229, Arg290, Asp293,and Tyr297 play a role in UDP-sugar binding
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: residues Ser123, Tyr147, Asn177, Asn197, Arg229, Arg290, Asp293,and Tyr297 play a role in UDP-sugar binding
Products: -
Products: -
r
UDP-D-glucose
UDP-D-galactose
-
Substrates: carbohydrate catabolism
Products: -
Products: -
r
UDP-D-glucose
UDP-D-galactose
-
Substrates: carbohydrate biosynthesis
Products: -
Products: -
r
UDP-D-glucose
UDP-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-D-xylose
UDP-L-arabinose
Substrates: the apparent equilibrium constant for UDP-Ara formation from UDP-Xyl is 0.89
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: RDH1 is a likely target of root-specific negative regulation by ethylene and loss of RDH1 function results in a heightened sensitivity of root tissues to both ethylene and auxin
Products: -
Products: -
?
UDP-galactose
UDP-glucose
-
Substrates: the bifunctional enzyme UDP-GlcNAc/Glc 4-epimerase is the sole supplier of the UDP-galactose and UDP-GalNAc required for synthesis of lipooligosaccharide
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: glycolysis and TCA cycle, Leloir pathway
Products: -
Products: -
?
UDP-galactose
UDP-glucose
-
Substrates: -
Products: -
Products: -
?
UDP-galactose
UDP-glucose
-
Substrates: role of the essential arginine residue in stretching and binding of the substrate
Products: -
Products: -
?
UDP-galactose
UDP-glucose
-
Substrates: enzyme catalyzes the first step of the Lelpoir pathway
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: galactose metabolic pathway
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: final step of the Leloir pathway
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: enzyme contributes to the Lelpoir pathway and also functions as a gatekeeper overseeing the ratios of important substrate pools required for the synthesis of glycosylated macromolecules
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: point mutations in UDP-galactose 4-epimerase are associated with the genetic disease, type III galactosemia
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: UDP-galacturonic acid C4-epimerase also interconverts UDP-galactose and UDP-glucose, albeit at much lower activity than the interconversion of UDP-galacturonate and UDP-glucuronic acid
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: -
Products: -
Products: -
?
UDP-galactose
UDP-glucose
Substrates: the apparent equilibrium constant for UDP-Gal formation from UDP-Glc is 0.24
Products: -
Products: -
r
UDP-galactose
UDP-glucose
-
Substrates: Leloir pathway of D-galactose catabolism
Products: -
Products: -
?
UDP-galactose
UDP-glucose
-
Substrates: Leloir pathway of galactose metabolism
Products: -
Products: -
r
UDP-galactose
UDP-glucose
Saccharomyces fragilis
-
Substrates: -
Products: -
Products: -
?
UDP-galactose
UDP-glucose
Substrates: glycolysis and TCA cycle, Leloir pathway
Products: -
Products: -
r
UDP-GalNAc
UDP-GlcNAc
-
Substrates: the bifunctional enzyme UDP-GlcNAc/Glc 4-epimerase is the sole supplier of the UDP-galactose and UDP-GalNAc required for synthesis of lipooligosaccharide. The enzyme supplies the UDP-GalNAc required for the synthesis of the capsule
Products: -
Products: -
r
UDP-GalNAc
UDP-GlcNAc
-
Substrates: enzyme contributes to the Lelpoir pathway and also functions as a gatekeeper overseeing the ratios of important substrate pools required for the synthesis of glycosylated macromolecules
Products: -
Products: -
r
UDP-GlcNAc
UDP-GalNAc
-
Substrates: wild-type enzyme shows no interconversion of UDP-GlcNAc and UDP-GalNAc, mutation Y299C results in a gain of activity against UDP-GalNAc by more than 230fold
Products: -
Products: -
r
UDP-glucose
UDP-galactose
Substrates: -
Products: -
Products: -
r
UDP-glucose
UDP-galactose
Substrates: -
Products: -
Products: -
r
UDP-glucose
UDP-galactose
Substrates: -
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
Substrates: epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
Substrates: epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose
Products: -
Products: -
r
additional information
?
-
-
Substrates: Leloir pathway of galactose metabolism
Products: -
Products: -
?
additional information
?
-
Q81JK4
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
Q81K34
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
Products: -
?
additional information
?
-
Q81JK4
Substrates: UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
Q81K34
Substrates: UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
Q81JK4
Substrates: no activity with UDP-N-acetylgalactoseamine
Products: -
Products: -
?
additional information
?
-
Q81K34
Substrates: no activity with UDP-N-acetylgalactoseamine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with UDP-N-acetylgalactoseamine
Products: -
Products: -
?
additional information
?
-
-
Substrates: TDP-[4-3H]glucose donates tritium to enzyme-bound NAD+, leading to formation of enzyme-[3H1]NADH. This suggests that a nucleoside diphospho-4-ulose of the configuration D-xylo-4-hexosulose is an intermediate in the reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: no interconversion of UDP-GalNAc and UDP-GlcNAc
Products: -
Products: -
?
additional information
?
-
Substrates: no 4-epimerization activity is found for allose, gulose, altrose, idose, mannose, and talose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no 4-epimerization activity is found for allose, gulose, altrose, idose, mannose, and talose
Products: -
Products: -
?
additional information
?
-
Substrates: Escherichia coli GalE is unable to catalyse the epimerization of acetylated substrates due to the so-called gatekeeper wall of the active site substrate-binding hexagonal box that is occupied by a bulky residue, Tyr299
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the interconversion of UDP-glucose and UDP-galactose during normal galactose metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: impairement of the enzyme results in galacosemia III that can lead to symptoms ranging from benign to severe
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme of galactose metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: the epimerase shows associated mutarotase activity distinct from the constitutively formed mutarotase activity. Both activities exist in two functionally independent domains
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays an essential role in exopolysaccharide formation. Exopolysaccharide synthesis is considerably improved at a controlled pH of 5.0 on galactose as carbon source, and is correlated with higher-induced activities of UDP-glucose pyrophosphorylase and UDP-galactose 4-epimerase under these growth conditions
Products: -
Products: -
?
additional information
?
-
Lacticaseibacillus casei CL 87
-
Substrates: the enzyme plays an essential role in exopolysaccharide formation. Exopolysaccharide synthesis is considerably improved at a controlled pH of 5.0 on galactose as carbon source, and is correlated with higher-induced activities of UDP-glucose pyrophosphorylase and UDP-galactose 4-epimerase under these growth conditions
Products: -
Products: -
?
additional information
?
-
Substrates: the bifunctional UDP-Glc 4-epimerase/UDP-Xyl 4-epimerase in the cytosol is distinct from the UDP-Xyl 4-epimerase in the Golgi apparatus, the two activities of UGE1 occur at the same catalytic site. No activity with UDP-N-acetylglucosamine or UDP-glucuronic acid, UGE1 substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2
Products: -
Products: -
?
additional information
?
-
Substrates: the type II enzyme also has UDP-GalNAc 4-epimerase activity, EC 5.1.3.7
Products: -
Products: -
?
additional information
?
-
Substrates: the type II enzyme also has UDP-GalNAc 4-epimerase activity, EC 5.1.3.7
Products: -
Products: -
?
additional information
?
-
-
Substrates: the type II enzyme also has UDP-GalNAc 4-epimerase activity, EC 5.1.3.7
Products: -
Products: -
?
additional information
?
-
Substrates: xylose-inducible gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: xylose-inducible gene
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the control of the biosynthesis of cell-wall polysaccharides containing D-galactose
Products: -
Products: -
?
additional information
?
-
-
Substrates: UDPgalactose 4-epimerase is a bifunctional enzyme with aldose 1-epimerase activity. The epimerase and mutarotase activities are located in different regions of the epimerase holoenzyme
Products: -
Products: -
?
additional information
?
-
Substrates: the bifunctional enzyme GAL10 also exhibits galactose mutarotase activity, EC 5.1.3.3
Products: -
Products: -
?
additional information
?
-
Saccharomyces cerevisiae ATCC 204508 / S288c
Substrates: the bifunctional enzyme GAL10 also exhibits galactose mutarotase activity, EC 5.1.3.3
Products: -
Products: -
?
additional information
?
-
Saccharomyces fragilis
-
Substrates: enzyme may play a regulatory role in controlling the flux of galactose metabolism
Products: -
Products: -
?
additional information
?
-
Substrates: Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: Uge1 protein contains only one epimerase domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: Uge1 protein contains only one epimerase domain
Products: -
Products: -
?
additional information
?
-
Substrates: Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: Uge1 protein contains only one epimerase domain
Products: -
Products: -
?
additional information
?
-
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
Products: -
Products: -
?
additional information
?
-
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
Products: -
Products: -
?
additional information
?
-
-
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
Products: -
Products: -
?
additional information
?
-
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
Products: -
Products: -
?
additional information
?
-
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
Products: -
Products: -
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
Products: -
Products: -
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp1 can use only UDP-Glc and UDP-Gal as substrates, and its conversion ratios are 30% and 10%, respectively
Products: -
Products: -
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
Products: -
Products: -
?
additional information
?
-
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
Substrates: two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. GalESp2 can convert both UDP-Glc/UDP-Gal and UDP-GlcNAc/UDP-GalNAc with conversion ratios of 29% and 28% for the UDP-Glc and UDP-GlcNAc substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively
Products: -
Products: -
?
additional information
?
-
-
Substrates: both enzymatic activities, as uridine diphosphate-galactose-4'-epimerase and UDP-N-acetylglucosamine-4'-epimerase, reveal that enzyme from Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-glucose to UDP-galactose and between their N-acetylated forms
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
XP_020276977.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
XP_006477432.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
CCQ00728.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
CCQ00728.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
XP_026409344.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-galactose
UDP-alpha-D-glucose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
XP_020276977.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: the NAD+-dependent enzyme is responsible for reversibly inverting the 4-hydroxyl configuration of UDP-alpha-D-galactose to form UDP-alpha-D-glucose
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: via 4-ketose intermediate
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Q81JK4, Q81K34
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
XP_006477432.1
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
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UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
CCQ00728.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
CCQ00728.1
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: anthocyanin biosynthesis
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
XP_026409344.1
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: Leloir pathway of membrane polysaccharide synthesis
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UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
Substrates: -
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
Substrates: -
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
Products: -
Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis
Products: -
Products: -
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: The enzyme UDP-glucose 4'-epimerase (GalE) interconverts UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).
Products: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: Galactose metabolism is essential for the survival of Trypanosoma brucei, the etiological agent of African sleeping sickness.
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Products: -
?
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
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r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
-
Substrates: -
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UDP-D-glucose
UDP-D-galactose
-
Substrates: carbohydrate catabolism
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r
UDP-D-glucose
UDP-D-galactose
-
Substrates: carbohydrate biosynthesis
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UDP-D-glucose
UDP-D-galactose
Substrates: -
Products: -
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UDP-galactose
UDP-glucose
-
Substrates: the bifunctional enzyme UDP-GlcNAc/Glc 4-epimerase is the sole supplier of the UDP-galactose and UDP-GalNAc required for synthesis of lipooligosaccharide
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UDP-galactose
UDP-glucose
-
Substrates: glycolysis and TCA cycle, Leloir pathway
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UDP-galactose
UDP-glucose
-
Substrates: enzyme catalyzes the first step of the Lelpoir pathway
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UDP-galactose
UDP-glucose
-
Substrates: galactose metabolic pathway
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UDP-galactose
UDP-glucose
-
Substrates: final step of the Leloir pathway
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UDP-galactose
UDP-glucose
-
Substrates: enzyme contributes to the Lelpoir pathway and also functions as a gatekeeper overseeing the ratios of important substrate pools required for the synthesis of glycosylated macromolecules
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UDP-galactose
UDP-glucose
-
Substrates: point mutations in UDP-galactose 4-epimerase are associated with the genetic disease, type III galactosemia
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UDP-galactose
UDP-glucose
-
Substrates: Leloir pathway of D-galactose catabolism
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UDP-galactose
UDP-glucose
-
Substrates: Leloir pathway of galactose metabolism
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UDP-galactose
UDP-glucose
Substrates: glycolysis and TCA cycle, Leloir pathway
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r
UDP-GalNAc
UDP-GlcNAc
-
Substrates: the bifunctional enzyme UDP-GlcNAc/Glc 4-epimerase is the sole supplier of the UDP-galactose and UDP-GalNAc required for synthesis of lipooligosaccharide. The enzyme supplies the UDP-GalNAc required for the synthesis of the capsule
Products: -
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r
UDP-GalNAc
UDP-GlcNAc
-
Substrates: enzyme contributes to the Lelpoir pathway and also functions as a gatekeeper overseeing the ratios of important substrate pools required for the synthesis of glycosylated macromolecules
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UDP-glucose
UDP-galactose
Substrates: -
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UDP-glucose
UDP-galactose
Substrates: -
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UDP-glucose
UDP-galactose
Substrates: -
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r
additional information
?
-
-
Substrates: Leloir pathway of galactose metabolism
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?
additional information
?
-
Q81JK4
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
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additional information
?
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Q81K34
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
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?
additional information
?
-
-
Substrates: the gene encodes a bifunctional enzyme with both UDP-GlcNAc 4-epimerase and UDP-Glc 4-epimerase activities and that no other annotated UDP-Glc 4-epimerase gene encodes a UDP-GlcNAc 4-epimerase
Products: -
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?
additional information
?
-
Q81JK4
Substrates: UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
Q81K34
Substrates: UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: UDP-N-acetylgalactoseamine 4-epimerase encoded by gene BAS5304 also shows UDP-glucose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: impairement of the enzyme results in galacosemia III that can lead to symptoms ranging from benign to severe
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?
additional information
?
-
-
Substrates: enzyme of galactose metabolism
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?
additional information
?
-
-
Substrates: during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
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?
additional information
?
-
Substrates: xylose-inducible gene
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?
additional information
?
-
-
Substrates: xylose-inducible gene
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?
additional information
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-
-
Substrates: the enzyme is involved in the control of the biosynthesis of cell-wall polysaccharides containing D-galactose
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?
additional information
?
-
Saccharomyces fragilis
-
Substrates: enzyme may play a regulatory role in controlling the flux of galactose metabolism
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?
additional information
?
-
Substrates: Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
Products: -
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?
additional information
?
-
-
Substrates: Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: Gal10p, a Gal-1-P uridylyltransferase, also shows UDP-glucose/-galactose 4-epimerase activity, overview
Products: -
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?
additional information
?
-
-
Substrates: both enzymatic activities, as uridine diphosphate-galactose-4'-epimerase and UDP-N-acetylglucosamine-4'-epimerase, reveal that enzyme from Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-glucose to UDP-galactose and between their N-acetylated forms
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
Torulopsis candida
-
depends on addition of NAD+ for catalytic acitivity, Km: 0.14 mM. Cannot be replaced by NADP+
NAD+
-
absolute requirement for NAD+. Km: 0.27 mM for the liver enzyme, Km: 0.28 mM for the mammary enzyme
NAD+
-
two nicotinamide cofactors bind in symmetry-related positions in the dimer
NAD+
-
NAD+ is very tightly but noncovalently bound in the active site, NAD+ is reduced to NADH in the course of catalysis. 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
NAD+
-
the amino acid side chains responsible for anchoring the NAD+ to the protein include Asp33, Asn37, Asp66, Tyr157 and Lys161
NAD+
coenzyme is tightly bound at the active site. NAD+ functions as the coenzyme for the interconversion of UDP-galactose and UDP-glucose by reversibly mediating their dehydrogenation to the common intermediate UDP-4-ketohexopyranoside. NAD+ activation induced by uridine nucleotides is brought about by a conformational change of epimerase that repositions Tyr149 at an increased distance from nicotinamide N1 of NAD+ while maintaining the electrostatic repulsion between Lys153 and nicotinamide N1 of NAD+
NAD+
-
1.78 mol of NAD+ per dimer. Each subunit is independently capable of being associated with one molecule of NAD+, suggestive of two NAD+ binding sites of epimerase per dimer
NAD+
-
the fully active GalE is dimeric and contains one tightly bound NAD+ per subunit, NAD+ undergoes reversible reduction to NADH in the chemical mechanism, practically irreversible binding of NAD+ within a Rossmann-type fold, nonstereospecific hydride transfer, uridine nucleotide-induced activation of NAD, Tyr149 as a base catalyst, and [GalE-NADH]-oxidation in one-electron steps by one-electron acceptors. pH-Dependent charge transfer complex between Tyr149 and NAD+. Binding structure, overview
NAD+
-
the amino acids that interact with NADH are Asp31, Asn35, Ser36, Lys83, Asn98, Tyr147, and Lys151
NAD+
bound within the active site cleft, binding structure, overview
NAD+
two paired Rossmann folds tightly bind one NAD+ cofactor per subunit. In Escherichia coli GalE, the NAD+ interacts more extensively with the protein than is observed with other SDR enzymes. pH-Dependent charge transfer complex between Tyr149 and NAD+
NAD+
the NAD+ cofactor can be removed from human GalE without denaturation. Fewer protein-NAD+ contacts are observed in the crystal structure, which explains the reversible character of cofactor binding
NAD+
enzyme-bound, exogenous NAD+ does not appear to be a strong activator of enzyme activity, there is no significant difference in enzyme activity regardless of the presence and absence of NAD+
NAD+
the N-terminal domain harbors the conserved sequence GxxGxxG forming a modified Rossmann-fold involved in binding of the cofactor NAD+
NADH
-
the amino acids that interact with NADH are Asp31, Asn35, Ser36, Lys83, Asn98, Tyr147, and Lys151
additional information
an NAD+ binding motif is GGXGXXG, not required for activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
Li+
enzyme activity is 43.7 U/mg protein at a metal concentration of 1 mM
Mg2+
Mn2+
Zn2+
enzyme activity is 17.2 U/mg protein at a metal concentration of 1 mM
additional information
Mg2+
enzyme activity is 51.5 U/mg protein at a metal concentration of 1 mM
Mn2+
enzyme activity is 43.2 U/mg protein at a metal concentration of 1 mM
additional information
no metal ion requirement of the recombinant protein for either UDP-Glc 4-epimerase or UDP-Xyl 4-epimerase activity
additional information
the enzyme is not specifically dependent on divalent metal ions for its catalytic activity, negligible effects by Co2+, Mn2+, Mg2+, Zn2+, Ca2+, Cu2+, Fe2+, or Ni2+
additional information
-
the enzyme is not specifically dependent on divalent metal ions for its catalytic activity, negligible effects by Co2+, Mn2+, Mg2+, Zn2+, Ca2+, Cu2+, Fe2+, or Ni2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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-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
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
fructose 1,6-diphosphate
-
inhibition is enhanced by combination with UMP
Galactose plus UMP
-
strong inhibition in the presence of UMP, no inhibition by UMP or sugar alone
L-Xylose plus UMP or UDP
-
inactivation due to reduction of the epimerase NAD+
-
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
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
UDP-6-deoxygalactose
-
weak competitive inhibitor with respect to UDPgalactose
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
powerful competitive
5'-UMP
-
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
-
string competitive inhibitor. The enzyme contains 0.77 mol of 5'-UMP per dimer
5'-UMP
-
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
-
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
-
-
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
-
-
diethyldicarbonate
-
almost complete inhibition at 5 mM after 30 min incubation
diethyldicarbonate
-
reversal of inhibition by hydroxylamine. Modification of 1 essential histidine residue is responsible for loss in catalytic activity
galactose 6-phosphate
-
activation of the minor enzyme form; partial inhibition of major enzyme form
glucose 1-phosphate
-
partial inhibition of minor enzyme form, no effect on major enzyme form
glucose 1-phosphate
-
partial inhibition of minor enzyme form, no effect on major enzyme form
glucose plus UMP
-
strong inhibition in the presence of UMP, no inhibition by UMP or sugar alone
-
glucose plus UMP
-
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
-
L-arabinose
-
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
-
epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
L-Arabinose plus UMP or UDP
-
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
-
L-Arabinose plus UMP or UDP
-
inactivation due to reduction of the epimerase NAD+
-
NADH
-
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
-
no inactivation by p-chloromercuribenzoate
additional information
-
inhibited by combination of 100 microM NADH and 10 microM NAD+
-
additional information
-
no inactivation by the UDP-D-fucose or D-fucose alone or by UDP-D-fucose plus 5'-UMP
-
additional information
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
non-covalently bound, released from the enzyme after denaturation with aqueous ethanol. Each enzyme molecule contains one molecule of NAD+
additional information
-
does not require external NAD+ for activity
-
Galactose 1-phosphate
-
activation of minor enzyme form, no effect on major enzyme form
Galactose 1-phosphate
-
activation of minor enzyme form, no effect on major enzyme form
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cataract
A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.
Cataract
[Early childhood cataract in hereditary UDP-galactose-4-epimerase deficiency--a case report]
Cysts
Mutation of a UDP-glucose-4-epimerase alters nematode susceptibility and ethylene responses in Arabidopsis roots.
Fanconi Syndrome
Defective galactose oxidation in a patient with glycogen storage disease and Fanconi syndrome.
galactokinase deficiency
Laboratory diagnosis of galactosemia: a technical standard and guideline of the American College of Medical Genetics and Genomics (ACMG).
Galactosemias
A Case Study of Monozygotic Twins Apparently Homozygous for a Novel Variant of UDP-Galactose 4'-epimerase (GALE) : A Complex Case of Variant GALE.
Galactosemias
A new mass screening method of detecting UDP-galactose-4-epimerase deficiency.
Galactosemias
A specific enzymatic assay for the diagnosis of congenital galactosemia. II. The combined test with 4-epimerase.
Galactosemias
Altered cofactor binding affects stability and activity of human UDP-galactose 4'-epimerase: Implications for type III galactosemia.
Galactosemias
Assessment of galactose-1-phosphate uridyltransferase activity in cells and tissues.
Galactosemias
Characterization of two mutations associated with epimerase-deficiency galactosemia, by use of a yeast expression system for human UDP-galactose-4-epimerase.
Galactosemias
Coordinated movement, neuromuscular synaptogenesis and trans-synaptic signaling defects in Drosophila galactosemia models.
Galactosemias
Detection of UDP-galactose-4-epimerase deficiency in a galactosemia screening program.
Galactosemias
Developmental defects in a Caenorhabditis elegans model for type III galactosemia.
Galactosemias
Functional analysis of mutations in UDP-galactose-4-epimerase (GALE) associated with galactosemia in Korean patients using mammalian GALE-null cells.
Galactosemias
Functional characterization of the K257R and G319E-hGALE alleles found in patients with ostensibly peripheral epimerase deficiency galactosemia.
Galactosemias
Identification and characterization of a mutation, in the human UDP-galactose-4-epimerase gene, associated with generalized epimerase-deficiency galactosemia.
Galactosemias
In silico prediction of the effects of mutations in the human UDP-galactose 4'-epimerase gene: towards a predictive framework for type III galactosemia.
Galactosemias
Laboratory diagnosis of galactosemia: a technical standard and guideline of the American College of Medical Genetics and Genomics (ACMG).
Galactosemias
Liquid Chromatography-Tandem Mass Spectrometry Enzyme Assay for UDP-Galactose 4'-Epimerase: Use of Fragment Intensity Ratio in Differentiation of Structural Isomers.
Galactosemias
Molecular basis for severe epimerase deficiency galactosemia. X-ray structure of the human V94m-substituted UDP-galactose 4-epimerase.
Galactosemias
Molecular dynamics, residue network analysis, and cross-correlation matrix to characterize the deleterious missense mutations in GALE causing galactosemia III.
Galactosemias
The metastability of human UDP-galactose 4'-epimerase (GALE) is increased by variants associated with type III galactosemia but decreased by substrate and cofactor binding.
Galactosemias
The molecular basis of UDP-galactose-4-epimerase (GALE) deficiency galactosemia in Korean patients.
Galactosemias
[Effectiveness of the screening programme for galactosemia. New strategy in Poland]
Genetic Diseases, Inborn
Analysis of UDP-galactose 4'-epimerase mutations associated with the intermediate form of type III galactosaemia.
Genetic Diseases, Inborn
Assessment of galactose-1-phosphate uridyltransferase activity in cells and tissues.
Infections
Brucella melitensis 16M: characterisation of the galE gene and mouse immunisation studies with a galE deficient mutant.
Infections
Developmental defects in a Caenorhabditis elegans model for type III galactosemia.
Infections
Schistosoma Japonicum UDP-Glucose 4-Epimerase Protein Is Located on the Tegument and Induces Moderate Protection against Challenge Infection.
Liver Failure
A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.
Muscle Hypotonia
A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.
Neoplasms
Carbon Source Affects Synthesis, Structures, and Activities of Mycelial Polysaccharides from Medicinal Fungus Inonotus obliquus.
Neoplasms
DNA sequence-dependent variation in nucleosome structure, stability, and dynamics detected by a FRET-based analysis.
Neoplasms
Metabolic inhibition of mammalian uridine diphosphate galactose 4-epimerase in cell cultures and in tumor cells.
Neoplasms
Sequence-dependent nucleosome structure and stability variations detected by Förster resonance energy transfer.
Osteoarthritis
The critical role of UDP-galactose-4-epimerase in osteoarthritis: modulating proteoglycans synthesis of the articular chondrocytes.
Starvation
Functional complementation of a membrane transport deficiency in Saccharomyces cerevisiae by recombinant ND4 fusion protein.
Starvation
Galactose starvation in a bloodstream form Trypanosoma brucei UDP-glucose 4'-epimerase conditional null mutant.
Stomach Neoplasms
Overexpression of UDP-Glucose 4-Epimerase Is Associated with Differentiation Grade of Gastric Cancer.
Thrombocytopenia
Inherited thrombocytopenia associated with mutation of UDP-galactose-4-epimerase (GALE).
Thrombocytopenia
Myelodysplasia and deficiency of uridine diphosphate-galactose 4-epimerase.
Trypanosomiasis, African
The molecular dynamics of Trypanosoma brucei UDP-galactose 4'-epimerase: a drug target for African sleeping sickness.
Tuberculosis
Rv3634c from Mycobacterium tuberculosis H37Rv encodes an enzyme with UDP-Gal/Glc and UDP-GalNAc 4-epimerase activities.
udp-glucose 4-epimerase deficiency
A Case of UDP-Galactose 4'-Epimerase Deficiency Associated with Dyshematopoiesis and Atrioventricular Valve Malformations: An Exceptional Clinical Phenotype Explained by Altered N-Glycosylation with Relative Preservation of the Leloir Pathway.
udp-glucose 4-epimerase deficiency
A first case report of UDP-galactose-4'-epimerase deficiency in China: genotype and phenotype.
udp-glucose 4-epimerase deficiency
A new mass screening method of detecting UDP-galactose-4-epimerase deficiency.
udp-glucose 4-epimerase deficiency
A new method of screening for inherited disorders of galactose metabolism.
udp-glucose 4-epimerase deficiency
Detection of UDP-galactose-4-epimerase deficiency in a galactosemia screening program.
udp-glucose 4-epimerase deficiency
Laboratory diagnosis of galactosemia: a technical standard and guideline of the American College of Medical Genetics and Genomics (ACMG).
udp-glucose 4-epimerase deficiency
Molecular basis for severe epimerase deficiency galactosemia. X-ray structure of the human V94m-substituted UDP-galactose 4-epimerase.
udp-glucose 4-epimerase deficiency
Myelodysplasia and deficiency of uridine diphosphate-galactose 4-epimerase.
udp-glucose 4-epimerase deficiency
Reversal of UDP-galactose 4-epimerase deficiency of human leukocytes in culture.
udp-glucose 4-epimerase deficiency
Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDP-GalNAc 4-epimerase deficient mutant.
udp-glucose 4-epimerase deficiency
Uridine diphosphate galactose 4'-epimerase deficiency. IV. Report of eight cases in three families.
udp-glucose 4-epimerase deficiency
Uridine diphosphate galactose 4-epimerase deficiency.
udp-glucose 4-epimerase deficiency
Uridine diphosphate galactose 4-epimerase deficiency. II. Clinical follow-up, biochemical studies and family investigation.
Vaccinia
Expansion of the mammalian 3 beta-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose-4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.31
UDP-D-glucose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.03
UDP-alpha-D-galactose
DdUGE1, pH and temperature not specified in the publication
0.06
UDP-alpha-D-galactose
DdUGE2, pH and temperature not specified in the publication
1.6
UDP-alpha-D-galactose
-
pH and temperature not specified in the publication
0.55
UDP-alpha-D-glucose
DdUGE1, pH and temperature not specified in the publication
0.79
UDP-alpha-D-glucose
DdUGE2, pH and temperature not specified in the publication
2 - 6
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant Y149F
83
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant K153M
110
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant S124A
230
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme
260
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant S124T
0.057
UDP-D-galactose
recombinant enzyme UGE4, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase
0.068
UDP-D-galactose
recombinant enzyme UGE3, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase
0.087
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme UGE1, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase
0.095
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme UGE2, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDPGlc dehydrogenase
0.15
UDP-D-galactose
recombinant enzyme UGE5, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
0.29
UDP-D-galactose
50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme
0.048
UDP-galactose
-
wild type enzyme, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 37°C
0.1 - 0.13
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.17 - 0.22
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.19 - 0.22
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.2
UDP-galactose
-
mutant enzyme M284K, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 24°C
0.23 - 0.3
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
0.25
UDP-galactose
-
mutant enzyme M284K, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 37°C
0.258
UDP-galactose
-
recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase
0.38
UDP-galactose
-
wild type enzyme, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 24°C
0.5
UDP-galactose
-
wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
0.8
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
1
UDP-galactose
-
mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
0.09
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.13
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.19
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.56
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.76
UDP-glucose
-
values are indirectly determined from the Haldane relationship
0.146
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118S/G119S
0.243
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118A/G119A
0.316
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S279Y
0.362
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, wild-type enzyme
0.426
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant T117S
0.437
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S116A
0.14
UDPgalactose
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
additional information
additional information
Saccharomyces fragilis
-
classical hyperbolic kinetics with UDPgalactose, allosteric kinetics with UDPglucose
-
additional information
additional information
Saccharomyces fragilis
-
enzyme shows Michaelis kinetics with UDPgalactose as the substrate and allosteric kinetics with UDPglucose as the substrate
-
additional information
additional information
-
biphasic Michaelis-Menten kinetics, kinetic patterns, overview. Michaelis-Menten relationship of the monomeric epimerase shows hyperbolic dependency
-
additional information
additional information
kinetic analyis of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetic analyis of wild-type and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
UDP-alpha-D-galactose
DdUGE1, pH and temperature not specified in the publication
0.37
UDP-alpha-D-galactose
DdUGE2, pH and temperature not specified in the publication
0.073
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant Y149F
0.17
UDP-alpha-D-glucose
DdUGE1, pH and temperature not specified in the publication
0.37
UDP-alpha-D-glucose
DdUGE2, pH and temperature not specified in the publication
0.61
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant S124A
0.67
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant K153M
250
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant S124T
760
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme
9
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme
20
UDP-D-galactose
recombinant enzyme UGE4
27
UDP-D-galactose
recombinant enzyme UGE3
55
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme UGE2
64
UDP-D-galactose
recombinant enzyme UGE5
0.633
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
23 - 24
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
28 - 34
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
42 - 66
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
46
UDP-galactose
-
mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
89 - 101
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
115 - 128
UDP-galactose
-
Different enzyme concentrations give slight variations in activity.
116
UDP-galactose
-
wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
199.1
UDP-galactose
-
recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase
2 - 8
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 mM).
19
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 mM).
24
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 mM).
32
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 mM).
33
UDP-glucose
-
The approximate value is estimated from reaction velocities at saturating substrate concentrations (59 mM).
0.37
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118A/G119A
0.78
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118S/G119S
0.99
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S279Y
2.32
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S116A
2.5
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant T117S
2.62
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, wild-type enzyme
960
UDPgalactose
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.33
UDP-alpha-D-galactose
DdUGE1, pH and temperature not specified in the publication
4.5
UDP-alpha-D-galactose
DdUGE2, pH and temperature not specified in the publication
0.31
UDP-alpha-D-glucose
DdUGE1, pH and temperature not specified in the publication
0.47
UDP-alpha-D-glucose
DdUGE2, pH and temperature not specified in the publication
2.9
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant Y149F
5.5
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant S124A
8.1
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant mutant K153M
970
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant S124T
3400
UDP-alpha-D-glucose
-
pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme
103
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme UGE1, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
350
UDP-D-galactose
recombinant enzyme UGE4, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
397
UDP-D-galactose
recombinant enzyme UGE3, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
435
UDP-D-galactose
recombinant enzyme UGE5, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
578
UDP-D-galactose
recombinant Arabidopsis thaliana enzyme UGE2, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase
0.78
UDP-galactose
-
recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase
0.79
UDP-galactose
-
mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
46
UDP-galactose
-
mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
232
UDP-galactose
-
wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C
1.55
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118A/G119A
3.13
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S279Y
5.39
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant S116A
5.43
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant G118S/G119S
5.92
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, mutant T117S
6.61
UDP-N-acetyl-alpha-D-glucosamine
-
pH 7.5, 45°C, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.6 - 12
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
5.6
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
Trypanosoma brucei
-
-
12
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
Homo sapiens
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0054
purified recombinant enzyme GalESp1, pH 8.0, 37°C, substrate UDP-Glc
0.0183
purified recombinant enzyme GalESp2, pH 8.0, 37°C, substrate UDP-Glc
0.78
recombinant His-tagged enzyme, pH 8.0, 37°C, substrate UDP-glucose
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
16.7
specific activity of recombinant enzyme in cell lysate after expression in Escherichia coli
19.8
192.4
purified recombinant enzyme, pH 7.0, 80°C, substrate UDP-galactose
38.9
4.6
49
specific activity of recombinant enzyme after purification by a Ni-sepharose colum
53.3
69.7
purified recombinant enzyme, pH 7.0, 80°C, substrate UDP-glucose
7.2
recombinant His-tagged enzyme, pH 8.0, 37°C, substrate UDP-galactose
additional information
38.9
specific activity of recombinant enzyme after purification by a DEAE-sepharose FF column
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.3
-
activity of the wild-type enzyme is pH-independent in the pH-range of 5.5-9.3
8 - 9
8 - 9.5
8.5
8.6
8.7
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
pH 3.0: about 45% of maximal activity, pH 9.0: about 40% of maximal activity
5 - 10
6 - 9
6.5 - 9.5
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
7.5 - 9
-
pH 7.5: about 50% of maximal activity, pH 9.0: about 75% of maximal activity
7.5 - 9.5
pH 7.5: about 40% of maximal activity, pH 9.5: about 75% of maximal activity
5 - 10
pH 5.0: about 50% of maximal activity, pH 10: about 55% of maximal activity
6 - 9
pH 6.0: about 80% of maximal activit, pH 9.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
30
35
37
50
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 50
-
15°C: about 45% of maximal activity, 45°C: about 40% of maximal activity
30 - 100
5 - 42
-
5°C: about 60% of maximal activity, 42°C: about 75% of maximal activity
30 - 100
30°C: 53% of the maximal activity, 100°C: 90% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.67
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UGE1; i.e. Albuca bracteata or Ornithogalum longebracteatum
UniProt
brenda
UGE2; i.e. Albuca bracteata or Ornithogalum longebracteatum
UniProt
brenda
syncytia induced by nematode Heterodera schachtii
UniProt
brenda
-
-
-
brenda
variety Nipponbare fragile culm 24 (Osfc24) mutant
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
levels of HvUGE1 mRNA are low in day 1 and day 3 coleoptiles, increases approximately 28fold in day 5 coleoptiles
brenda
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
brenda
-
during fruit development, no significant correlation occurs between the changes in UGE activity and UDP-sugar contents, overview
brenda
expression of the enzyme is associated with gastric adenocarcinomas with well and moderately differentiated histological grades
brenda
expression of HvUGE1 is highest in leaf tips, rapidly decreases to very low levels in the basal region of the leaves
brenda
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
brenda
additional information
-
the gene is expressed in all tissues, with highest expression level in the stems and roots
brenda
-
Heterodera schachtii parasitism strongly downregulates RDH1 expression in the root 3 days after inoculation
brenda
mRNA levels of HvUGE1 are very high in the maturation zone compared with other regions of the root
brenda
-
the gene is expressed in all tissues, with highest expression level in the stems and roots
brenda
-
two UDP-Glc 4-epimerase genes: StUGE45 and StUGE51. StUGE51 shows higher expression than StUGE45
brenda
additional information
enzyme expression in relation to N levels in roots and shoots, overview
brenda
additional information
enzyme expression levels during different developmental stages evaluated by quantitative real-time reverse transcription PCR enzyme expression and immunohistochemic analysis, overview
brenda
additional information
-
enzyme expression levels during different developmental stages evaluated by quantitative real-time reverse transcription PCR enzyme expression and immunohistochemic analysis, overview
brenda
additional information
-
galE transcription exhibits a distinct expression profile under different culture conditions
brenda
additional information
-
galE transcription exhibits a distinct expression profile under different culture conditions
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the bifunctional UDP-Glc 4-epimerase/UDP-Xyl 4-epimerase, encoded by UGE1, in the cytosol is distinct from the UDP-Xyl 4-epimerase in the Golgi apparatus
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the GalE enzyme is a member of the extended short-chain dehydrogenase/reductase superfamily of proteins. It has the two signature sequences of the extended SDR superfamily, a GxxGxxG motif, which is located near the cofactor binding pocket, and a YxxxK motif, in which the conserved tyrosine plays a key role in catalysis, are strictly conserved in Xanthomonas GalE as well as several crystallized GalE proteins from other bacteria
evolution
-
UDP-hexose 4-epimerases belong to the superfamily of short-chain dehydrogenase/reductase group 2, which typically show a two-domain structure
evolution
bifunctional UDP-glucose 4-epimerases, UGEs, with UDP-xylose 4-epimerase (EC 5.1.3.5) activity are conserved in vascular plants
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa). Despite the relatively low sequence identity among all three groups, the similarity of the enzymes' tertiary structures is striking with an overall RMSD of the multiple structure alignment being 1.08 A and variation being most pronounced at the C-terminal end
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
evolution
presence of three putative UDP glucose-4-epimerases, UgeA, UgeB, and UgeC, in Aspergillus niger, encoded by genes An14g03820, An12g10410, and An02g11320. Enzyme UgeA belongs to the NAD(P)-dependent epimerase/dehydratase family
evolution
the rice genome contains four putative UGE-encoding genes (OsUGE1-4). All four predicted OsUGEs in rice carry an epimerase domain and belong to the NAD+ dependent epimerase/dehydratase family proteins that use NAD+ as a cofactor and nucleotide-sugars as substrates. Expression profiles of UGEs in Oryza sativa support distinct in planta roles throughout development
evolution
sugar nucleotide epimerases, including UDP-Gal/Glc 4-epimerase, are a class of enzymes that belong to the extended SDR subfamily of the short chain dehydrogenase reductase (SDR) superfamily, enzyme Rv3634c belongs to the NAD+-dependent epimerase/dehydratase family of proteins (accession no. PF01370)
evolution
UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp1 is a group 1 enzyme, GalE enzymes belonging to group 1 contain LSYNHL or KSYNNY in the amino acid sequences
evolution
UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp2 is a group2 enzyme, GalE enzymes belonging to group 2 contain KSYNNC
evolution
the epimerase and dehydratase Ab-WbjB belongs to the extended short-chain dehydrogenase/reductase (SDR) family, related in fold to previously characterised enzymes CapE and FlaA1
evolution
overview of the molecular evolution and structural basis for the substrate specificity
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
XP_020276977.1
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
XP_026409344.1
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
XP_006477432.1
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
-
the UGE mRNA sequences from monocotyledons, dicotyledons, bryophyte, pteridophyte, and phycophytas are obviously distinct
evolution
-
sugar nucleotide epimerases, including UDP-Gal/Glc 4-epimerase, are a class of enzymes that belong to the extended SDR subfamily of the short chain dehydrogenase reductase (SDR) superfamily, enzyme Rv3634c belongs to the NAD+-dependent epimerase/dehydratase family of proteins (accession no. PF01370)
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evolution
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the GalE enzyme is a member of the extended short-chain dehydrogenase/reductase superfamily of proteins. It has the two signature sequences of the extended SDR superfamily, a GxxGxxG motif, which is located near the cofactor binding pocket, and a YxxxK motif, in which the conserved tyrosine plays a key role in catalysis, are strictly conserved in Xanthomonas GalE as well as several crystallized GalE proteins from other bacteria
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evolution
Saccharomyces cerevisiae ATCC 204508 / S288c
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UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
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evolution
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
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UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp1 is a group 1 enzyme, GalE enzymes belonging to group 1 contain LSYNHL or KSYNNY in the amino acid sequences
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evolution
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
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UDP-hexose 4-epimerases belong to the superfamily of short-chain/reductase having two-domain structure. The N-terminal domain with conserved sequence GxxGxxG forms a modified Rossmann-fold and is involved in binding of the cofactor NAD+, whereas a smaller domain with conserved sequence YxxxK is involved in substrate binding. Both functional motifs conserved in the SDR superfamily members are identified in GalESp1 and GalESp2. Based on its substrate specificity, GalEs can be divided into three groups. Group 1 epimerases strongly prefer non-acetylated substrates (UDP-Glc/Gal), with a corresponding Y300 residue. Group 2 epimerases can epimerize both acetylated (UDP-GlcNAc/GalNAc) and non-acetylated substrates. Group 3 epimerases show a strong preference for acetylated substrates with a corresponding G86 residue. GalESp2 is a group2 enzyme, GalE enzymes belonging to group 2 contain KSYNNC
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evolution
-
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
-
evolution
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
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UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
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evolution
Aspergillus niger CBS 513.88 / FGSC A1513
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presence of three putative UDP glucose-4-epimerases, UgeA, UgeB, and UgeC, in Aspergillus niger, encoded by genes An14g03820, An12g10410, and An02g11320. Enzyme UgeA belongs to the NAD(P)-dependent epimerase/dehydratase family
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evolution
Acinetobacter baumannii Dl279779
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the epimerase and dehydratase Ab-WbjB belongs to the extended short-chain dehydrogenase/reductase (SDR) family, related in fold to previously characterised enzymes CapE and FlaA1
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malfunction
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GALE deficiency leads to mild or severe disease with clinical symptoms similar to classical galactosemia
malfunction
UDP-galactose-4-epimerase deficiency causes galactosemia. Altered protein stability is due to misfolding and loss or reduction of enzyme activity is responsible for the molecular defects underlying GALE-deficiency galactosemia
malfunction
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In the absence of Uge5, Uge3 activity is sufficient for growth on galactose and the synthesis of galactosaminogalactan containing lower levels of galactose but not the synthesis of galactofuranose. A double deletion of uge5 and uge3 blocked growth on galactose and synthesis of both galactofuranose and galactosaminogalactan, phenotypes, overview
malfunction
the S306Y mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates, which results in the observed loss of activity
malfunction
the replacement of the double glycine motif, observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box, by a single alanine or serine as seen in the other UDP-hexose epimerases results in a strongly reduced specific activity and turnover number
malfunction
mutation of enzyme UgeA results in reduced galactofuranose production, deletion of gene ugeA abolishes the galactofuranose production
malfunction
enzyme overexpressing mutant OsUGE1-OX lines maintain 18-24% more sucrose and 12-22% less cellulose in shoots compared to wild-type when subjected to suboptimal N-levels. OsUGE1-OX lines maintain proportionally more galactose and glucose in the hemicellulosic polysaccharide profile of plants compared to wild-type plants when grown under low N. The altered cell wall C-partitioning during N-limitation in the OsUGE1-OX lines appears to be mediated by OsUGE1 via the repression of the cellulose synthesis associated genes, OsSus1, OsCesA4, 7, and 9. OsUGE1 shows phenotypic alteration at carbohydrate partitioning level in the transgenic lines, overexpressinon phenotypes, overview
malfunction
mutations S121A and Y146F lead to complete loss of activity whereas mutation K150R leads to partial loss of activity. There are no gross changes in the secondary structures of any of these three mutants
malfunction
silencing GALE gene with specific siRNAs results in a markedly inhibition of proteoglycans (PGs)synthesis in human articular chondrocytes. GALE protein levels are also decreased in both human osteoarthritis cartilage, thus leading to losses of PGs contents. GALE inhibition might contribute to osteoarthritis progress. Mutations of gene GALE in humans results in an inherited metabolic disease, the type III galactosemia
malfunction
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides. Importantly, these defects including aggregate formation are restored by supplementation of D-galactose in the medium. Intracellular aggregates in the uge4 mutant contains endomembrane markers in the secretory and vacuolar pathways. The lack of UGE4 function affects the structure of the endoplasmic reticulum or trafficking of the endoplasmic reticulum marker. Phenotype, overview. Disruption of the cytoskeleton is not a primary cause of the endomembrane aggregates in the uge4 mutant
malfunction
mutation in OsUGE2 considerably affects cellulose biosynthesis, leading to reduced lignocellulose recalcitrance
malfunction
CRISPR/Cas9-mediated GALE deletion in human cells triggers major imbalances in nucleotide sugars and dramatic changes in glycolipids and glycoproteins, including a subset of integrins and the cell surface death receptor FS-7-associated surface antigen. Substantial decreases in total sialic acid, galactose, and GalNAc levels in glycans are observed. These changes also directly impacted cell signaling, as GALE-/- cells exhibited FS-7-associated surface antigen ligand-induced apoptosis
malfunction
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mutations S121A and Y146F lead to complete loss of activity whereas mutation K150R leads to partial loss of activity. There are no gross changes in the secondary structures of any of these three mutants
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malfunction
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identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides. Importantly, these defects including aggregate formation are restored by supplementation of D-galactose in the medium. Intracellular aggregates in the uge4 mutant contains endomembrane markers in the secretory and vacuolar pathways. The lack of UGE4 function affects the structure of the endoplasmic reticulum or trafficking of the endoplasmic reticulum marker. Phenotype, overview. Disruption of the cytoskeleton is not a primary cause of the endomembrane aggregates in the uge4 mutant
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malfunction
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In the absence of Uge5, Uge3 activity is sufficient for growth on galactose and the synthesis of galactosaminogalactan containing lower levels of galactose but not the synthesis of galactofuranose. A double deletion of uge5 and uge3 blocked growth on galactose and synthesis of both galactofuranose and galactosaminogalactan, phenotypes, overview
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malfunction
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
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the replacement of the double glycine motif, observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box, by a single alanine or serine as seen in the other UDP-hexose epimerases results in a strongly reduced specific activity and turnover number
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malfunction
Aspergillus niger CBS 513.88 / FGSC A1513
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mutation of enzyme UgeA results in reduced galactofuranose production, deletion of gene ugeA abolishes the galactofuranose production
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metabolism
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UgeA interconverts UDP-glucose and UDP-galactose and participates in galactose metabolism
metabolism
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GALE catalyzes the third step of the Leloir pathway of galactose metabolism
metabolism
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the galE gene product is not the only enzyme responsible for UDP-glucose production in the organism
metabolism
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overlapping and distinct roles of UDP-glucose 4-epimerases in galactose metabolism and the synthesis of galactose-containing cell wall polysaccharides, galactosaminogalactan synthesis requires the UDP-glucose 4-epimerases, Uge5 and Uge3, whereas galactomannan synthesis requires Uge5 alone, overview
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
metabolism
the enzyme catalyzes the third step of the Leloir pathway in galactose metabolism
metabolism
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in addition to the biosynthetic role of UGE in carbohydrate synthesis, the enzyme is also a pivotal part of the Leloir pathway, which metabolizes galactose through glycolysis
metabolism
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overlapping and distinct roles of UDP-glucose 4-epimerases in galactose metabolism and the synthesis of galactose-containing cell wall polysaccharides, galactosaminogalactan synthesis requires the UDP-glucose 4-epimerases, Uge5 and Uge3, whereas galactomannan synthesis requires Uge5 alone, overview
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metabolism
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the galE gene product is not the only enzyme responsible for UDP-glucose production in the organism
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metabolism
Saccharomyces cerevisiae ATCC 204508 / S288c
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UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
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metabolism
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UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
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metabolism
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
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UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
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metabolism
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
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the enzyme is involved in D-galactose metabolism
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physiological function
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enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis, gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
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galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
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galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis
physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
bifunctional cytosolic UDP-glucose 4-epimerase catalyses the interconversion between UDP-D-xylose and UDP-L-arabinose in plants
physiological function
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GalE plays a key role in lipopolysaccharide biosynthesis
physiological function
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UDP-Gal provides all galactosyl units in biologically synthesized carbohydrates. All healthy cells produce UDP-Gal from uridine 5'-diphospho-alpha-D-glucose UDP-Glc, by the action of UDP-galactose 4-epimerase
physiological function
the enzyme produces the precursor UDP-galactopyranose required for galactofuranose synthesis
physiological function
the enzyme induces moderate protection against challenge infection
physiological function
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Uge5 is the dominant UDP-glucose 4-epimerase in Aspergillus fumigatus and is essential for normal growth in galactose-based medium. Uge5 is required for synthesis of the galactofuranose component of galactomannan and contributes galactose to the synthesis of galactosaminogalactan. Uge3 can mediate production of both UDP-galactose and UDP-N-acetylgalactosamine, cf. EC 5.1.3.7, and is required for the production of galactosaminogalactan but not galactomannan
physiological function
the enzyme is involved in the biosynthesis of anti-tumor polysaccharides in Ornithogalum caudatum. UGE also plays a key role in carbohydrate partitioning, plant growth and development. Enzyme UGE is important in the composition of the sugar nucleotide pools
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures, such as capsular polysaccharide (CPS)
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of other polysaccharide structures, such as proteoglycans (PGs) of articular chondrocytes. Secondary role of the human enzyme is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc)
physiological function
UDP-galactose 4-epimerase plays an essential role in development and homeostasis of Drosophila that extends beyond the Leloir pathway. UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of other polysaccharide structures, such as capsular polysaccharide (CPS), or extracellular polysaccharide (EPS) from Streptococcus thermophilus, one of the most widely used bacteria in the dairy industry
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
physiological function
enzyme UgeA is required for the biosynthesis of galactofuranose as well as for galactose metabolism in Aspergillus niger. UgeA is required for growth on galactose in Aspergillus niger
physiological function
enzyme OsUGE1 plays an important role in carbohydrate partitioning to the cell wall in Oryza sativa
physiological function
UDP-Gal/GalNAc epimerases differ from each other in their substrate specificity with respect to the utilization of N-acetylated derivatives and are accordingly classified into three types viz., type I, type II and type III. Type I enzymes utilize only UDP-Glc/Gal as substrates whereas Type III enzymes use only UDP-GlcNAc/GalNAc as substrates. Type II enzymes can utilize both as substrates
physiological function
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
physiological function
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1
physiological function
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1
physiological function
UDP-galactose-4-epimerase (GALE) is a key enzyme catalyzing the interconversion of UDP-glucose and UDP-galactose, as well as UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine, which are all precursors for the proteoglycans (PGs) synthesis. Role of GALE in PGs synthesis of human articular chondrocytes, the GALE expression in osteoarthritis, and the regulation of GALE expression by interleukin-1beta, overview. GALE mRNA expression is stimulated by interleukin-1beta in early phase, but suppressed in late phase, while the suppression of GALE expression induced by interleukin-1beta is mainly mediated by stress-activated protein kinase/c-Jun N-terminal kinase pathway. Both SAP/JNK inhibitor SP600125 and p38 MAPK inhibitor SB203580 attenuate the suppression of interleukin-1beta on GAG synthesis and GALE mRNA expression of chondrocyte. Critical role of GALE in maintaining cartilage homeostasis
physiological function
UDP-D-galactose synthesis by UDP-glucose 4-epimerase 4 is required for organization of the trans-Golgi network/early endosome in Arabidopsis thaliana root epidermal cells. UDP-D-galactose synthesis by UGE4 is important for endomembrane organization in addition to cell wall structure
physiological function
the enzyme is involved in the biosynthesis of anti-tumor polysaccharides in Ornithogalum caudatum. UXE also plays a key role in carbohydrate partitioning, plant growth and development. Enzyme UXE is important in the composition of the sugar nucleotide pools
physiological function
the enzyme acts on protein and lipid glycosylation in normal and neoplastic cells
physiological function
the enzyme (GalE) generates UDP-Gal for galactose extension by Lic2A
physiological function
suppression of alternative lipooligosaccharide glycosyltransferase activity by UDP-galactose epimerase enhances murine lung infection and evasion of serum IgM
physiological function
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overexpression of the uxe gene suppresses the phenotypes of an exoB mutant, evidencing that Uxe can functionally replace ExoB. Under conditions stimulating expression of the arabinose containing polysaccharide (APS) biosynthesis operon, Uxe contributes to the synthesis of multiple glycans and thereby to cell protection, biofilm formation, and symbiosis
physiological function
the enzyme (OsUGE2) participates in distinct metabolic pathways to co-modulate cellulose biosynthesis and wall assembly by dynamically providing UDP-alpha-D-galactose and UDP-alpha-D-glucose substrates. The enzyme (OsUGE2) mainly has enzyme activity in providing UDP-alpha-D-galactose as the substrate for the biosynthesis of arabinogalactan protein and chloroplast galactolipids
physiological function
the major structural proteins (archaellins) of the archaellum are glycoproteins, modified with N-linked tetrasaccharides that are essential for the proper assembly and function of archaella. The enzyme (AglW) plays a key role in the synthesis of the tetrasaccharide
physiological function
universal enzyme responsible for interconversion of UDP-glucose and UDP-galactose
physiological function
the enzyme is required for cell-surface glycome structure and has a functional role of GALE-mediated nucleotide sugar regulation in death receptor signaling. It may have implications for the molecular etiology of illnesses characterized by NS imbalances, including galactosemia and metabolic syndrome
physiological function
Gne is the enzyme providing Gal and GalNAc residues with the synthesis of all three cell-surface carbohydrates in Campylobacter jejuni NCTC 11168, the capsule, the Pgl heptasaccharide, and the lipooligosaccharide (LOS)
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
XP_020276977.1
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme catalyzes one of the initial steps in O-antigen biosynthesis
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
XP_026409344.1
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
XP_006477432.1
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
-
the enzyme can improve the resistance of plants to certain abiotic stress, including drought, salt, freezing, and osmotic stress. The enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, which is a rate-limiting step for polysaccharides biosynthesis. As the main cell wall materials, polysaccharides play an irreplaceable role throughout the whole life history of plant
physiological function
WbpP is an enzyme essential for B-band lipopolysaccharide production in serotype O6
physiological function
-
UDP-Gal/GalNAc epimerases differ from each other in their substrate specificity with respect to the utilization of N-acetylated derivatives and are accordingly classified into three types viz., type I, type II and type III. Type I enzymes utilize only UDP-Glc/Gal as substrates whereas Type III enzymes use only UDP-GlcNAc/GalNAc as substrates. Type II enzymes can utilize both as substrates
-
physiological function
-
UDP-D-galactose synthesis by UDP-glucose 4-epimerase 4 is required for organization of the trans-Golgi network/early endosome in Arabidopsis thaliana root epidermal cells. UDP-D-galactose synthesis by UGE4 is important for endomembrane organization in addition to cell wall structure
-
physiological function
-
the enzyme (GalE) generates UDP-Gal for galactose extension by Lic2A
-
physiological function
-
suppression of alternative lipooligosaccharide glycosyltransferase activity by UDP-galactose epimerase enhances murine lung infection and evasion of serum IgM
-
physiological function
-
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
-
physiological function
-
Uge5 is the dominant UDP-glucose 4-epimerase in Aspergillus fumigatus and is essential for normal growth in galactose-based medium. Uge5 is required for synthesis of the galactofuranose component of galactomannan and contributes galactose to the synthesis of galactosaminogalactan. Uge3 can mediate production of both UDP-galactose and UDP-N-acetylgalactosamine, cf. EC 5.1.3.7, and is required for the production of galactosaminogalactan but not galactomannan
-
physiological function
-
Gne is the enzyme providing Gal and GalNAc residues with the synthesis of all three cell-surface carbohydrates in Campylobacter jejuni NCTC 11168, the capsule, the Pgl heptasaccharide, and the lipooligosaccharide (LOS)
-
physiological function
-
overexpression of the uxe gene suppresses the phenotypes of an exoB mutant, evidencing that Uxe can functionally replace ExoB. Under conditions stimulating expression of the arabinose containing polysaccharide (APS) biosynthesis operon, Uxe contributes to the synthesis of multiple glycans and thereby to cell protection, biofilm formation, and symbiosis
-
physiological function
Saccharomyces cerevisiae ATCC 204508 / S288c
-
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
-
physiological function
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
-
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc, EC 5.1.3.7. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1
-
physiological function
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
-
UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. GalE is a key enzyme for the processes of eukaryotic and prokaryotic protein glycosylation and the production or secretion of virulence factors in many bacterial pathogens. It is an important virulence factor in many bacterial pathogens. The two genes, galEsp1 and galEsp2, are responsible for galactose metabolism in pathogenic Streptococcus pneumoniae TIGR4. Both GalESp1 and GalESp2 catalyze the epimerization of UDP-Glc/UDP-Gal, but only GalESp2 catalyzes the epimerization of UDP-GlcNAc/UDP-GalNAc. Enzyme GalESp2 has a 3fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1
-
physiological function
-
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
-
physiological function
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
-
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
-
physiological function
Aspergillus niger CBS 513.88 / FGSC A1513
-
enzyme UgeA is required for the biosynthesis of galactofuranose as well as for galactose metabolism in Aspergillus niger. UgeA is required for growth on galactose in Aspergillus niger
-
physiological function
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
-
additional information
-
ligand-bound enzyme structures, active site structure including Lys153, Tyr149, and Ser124, overview
additional information
-
putative GalE catalytic residues are Ser124, Tyr147, and Lys151
additional information
ligand binding structures, docking study, overview
additional information
-
ligand binding structures, docking study, overview
additional information
-
structure homology modeling, overview. The Marinithermus enzyme makes use of a TxnYx3K catalytic triad rather than the usual SxnYx3K triad. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine, the gatekeeper residue is responsible for the substrate specificity, the two consecutive glycine residues, Gly118 and Gly119, are a unique feature of GalE enzymes from Thermus species and important for activity as well as affinity
additional information
enzyme structure and substrate specificity, structure-function relationship, overview. Comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes
additional information
comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. The human enzyme has a smaller active site, explaining the secondary role of the human enzyme, which is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc). Activity on the larger acetylated substrates requires a larger active site
additional information
-
comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. The human enzyme has a smaller active site, explaining the secondary role of the human enzyme, which is epimerization of UDP-N-acetylgalactosamine (UDP-Gal-NAc). Activity on the larger acetylated substrates requires a larger active site
additional information
comparison of the hexagonal box model of sugar-binding pockeets of several GalE enzymes
additional information
comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. A unique double glycine motif is observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box important for substrate specificity
additional information
Ser121 and Tyr146 are essential for epimerase activity of Rv3634c. The catalytic triad consisting of Ser, Tyr and Lys carries out proton transfer from nucleotide sugar to NAD+ and back, thus effecting the epimerization of the substrate
additional information
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
additional information
-
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
additional information
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
-
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
additional information
-
Ser121 and Tyr146 are essential for epimerase activity of Rv3634c. The catalytic triad consisting of Ser, Tyr and Lys carries out proton transfer from nucleotide sugar to NAD+ and back, thus effecting the epimerization of the substrate
-
additional information
-
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
-
additional information
-
putative GalE catalytic residues are Ser124, Tyr147, and Lys151
-
additional information
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
-
the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2
-
additional information
-
comparison of the hexagonal box model of sugar-binding pockeets of several GalE enzymes
-
additional information
Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1
-
comparison of the hexagonal box model of sugar-binding pockets of several GalE enzymes. A unique double glycine motif is observed right next to the conserved serine/threonine (T117) that is part of the hexagonal box important for substrate specificity
-
additional information
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
-
Show AA Sequence and Transmembrane Helices (29636 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
103000
-
Dynamic Light Scattering, calculated from the hydrodynamic radius using the default volume shape hydration model.
120000
160000
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker, dimeric form, gel filtration
183000 - 187000
-
sucrose density gradient centrifugation, gel filtration
240000
-
sedimentation equilibrium measurement, addition of NAD+, 0.01 M Tris buffer with cations, active tetrameric form
320000
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker, tetrameric form, gel filtration
35000
37000
38000
39000
40000
40600
42000
60000
70000
75000
78000
79000
80000
84000
-
Dynamic Light Scattering, calculated from the hydrodynamic radius using the default volume shape hydration model.
91000
-
Dynamic Light Scattering, calculated from the hydrodynamic radius using the default volume shape hydration model.
98000
-
Dynamic Light Scattering, calculated from the hydrodynamic radius using the default volume shape hydration model.
120000
-
sedimentation equilibrium measurement, addition of NAD+, active dimeric enzyme form
39000
-
1 * 39000, subunits of the dimeric epimerase are stabilized under certain conditions where they can function catalytically
60000
-
2 * 60000, enzyme exists in an active dimeric and an active tetrameric form
60000
-
4 * 60000, enzyme exists in an active dimeric and an active tetrameric form
80000
-
2 * 80000, fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker exist as monomeric, dimeric and tetrameric form. The monomeric form has low epimerase activity, SDS-PAGE
80000
-
4 * 80000, fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker exist as monomeric, dimeric and tetrameric form. The monomeric form has low epimerase activity, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
monomer
tetramer
additional information
?
x * 38000, about, recombinant His-tagged enzyme, SDS-PAGE
?
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
-
x * 38000, about, recombinant His-tagged enzyme, SDS-PAGE
-
dimer
-
2 * 80000, fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker exist as monomeric, dimeric and tetrameric form. The monomeric form has low epimerase activity, SDS-PAGE
dimer
-
wild-type protein and all the mutants (N34S, G90E, V94M, D103G, L183P, K257R, L313M, G319E and R335H) are able to form dimers. In all cases, especially with the mutant proteins, some higher molecular mass species are also observed
dimer
-
2 * 60000, enzyme exists in an active dimeric and an active tetrameric form
dimer
-
The resulting model is composed of four subunits forming two physiological dimers (subunits AB and CD). Subunit A comprises residues -1150, 157237 and 249381, subunit B residues -1150, 158235 and 249381, subunit C residues -1152, 158237 and 248381 and subunit D residues -1150, 157235 and 249381.The -1 refers to a serine residue which precedes the initiating methionine and is an artifact of the expression plasmid that generates an N-terminal extension. There are several missing residues which belong to flexible surface loops. Each active site is occupied by well ordered NAD+ and UDP-FGal.
hexamer
enzyme Ab-WbjB is a hexamer, organised into a trimer of chain pairs, with coenzyme NADP+ occupying each chain
hexamer
Acinetobacter baumannii Dl279779
-
enzyme Ab-WbjB is a hexamer, organised into a trimer of chain pairs, with coenzyme NADP+ occupying each chain
-
homodimer
-
a homodimer, containing one catalytic site and one NAD+ as cofactor per subunit, not showing fast association-dissociation
homodimer
2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation
homodimer
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
2 * 34899, calculated from sequence
-
homodimer
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation
-
homodimer
-
2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation
-
monomer
-
2 * 80000, fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker exist as monomeric, dimeric and tetrameric form. The monomeric form has low epimerase activity, SDS-PAGE
monomer
-
1 * 39000, subunits of the dimeric epimerase are stabilized under certain conditions where they can function catalytically
tetramer
-
4 * 80000, fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker exist as monomeric, dimeric and tetrameric form. The monomeric form has low epimerase activity, SDS-PAGE
tetramer
-
4 * 60000, enzyme exists in an active dimeric and an active tetrameric form
additional information
the enzyme has an N-terminal nucleotide binding domain and a smaller C-terminal domain that is responsible for the correct positioning of its substrate, a UDP-sugar. The N-terminal domain comprises seven parallel beta-strands that are flanked on both sides by alpha-helices and shape the Rossmann fold. Two paired Rossmann folds tightly bind one NAD+ cofactor per subunit
additional information
determination of the structure of human UDP-Gal 4-epimerase. The C-terminal domain is built from five beta-strands and four alpha-helices
additional information
-
determination of the structure of human UDP-Gal 4-epimerase. The C-terminal domain is built from five beta-strands and four alpha-helices
additional information
-
sequence comparisons and structure homology modeling, overview. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine
additional information
enzyme secondary structure analysis using circular dichroism
additional information
-
enzyme secondary structure analysis using circular dichroism
-
additional information
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
enzyme structure analysis, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme Ab-WbjB, hanging drop vapour diffusion method, in an 1:1 ratio mixture from 0.2 M NaCl, 0.1 M HEPES, pH 5.6, and 25% v/v PEG 3350, X-ray diffraction structure determination and analysis at 2.64-2.70 A, method optimization, overview, molecular replacement using the structure of Helicobacter pylori FlaA1 (PDB ID 2gn4) as template
purified recombinant enzyme in complex with UDP-galactose using the microbatch method, 15 mg/ml protein in 25 mM Tris, pH 8, is used with crystallization solution containing 20% w/v PEG 3350, 0.1 M Bis-Tris propane, pH 7.5, and 0.2 M sodium fluoride, 2 weeks, X-ray diffraction structure determination and analysis at 2.4 A resolution
purified recombinant His-tagged enzyme, microbatch method, 4°C, mixing of equal volumes of protein and precipitant solution, the latter containing 20% w/v PEG 3350, 0.1 M Bis-Tris propane pH 7.5, 0.2 M sodium fluoride, cryoprotection with 25% glycerol, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement
crystals of bGalE are grown at 4°C using the sitting drop vapor diffusion method. Crystal structures of the enzyme are determined in three ternary complex forms: NAD+/UDP, NAD+/UDP-GlcNAc, and NAD+/UDP-Glc
crystal structure of the oxidized and reduced forms of UDP-galactose 4-epimerase
crystal structure of the ternary complex of UDP-galactose 4-epimerase with NADH and UDP-phenol
-
suitable crystallization conditions are both at room temperature and at 4°C using sparse matrix screen and the hanging drop method of vapor diffusion. The best crystals are observed growing from polyethylene glycol 8000 and potassium chloride and in the presence of 2 mM NAD+. Typical large crystals are ontained from 18-20% polyethylene glycol 8000, 100 mM Hepes, pH 7.5, and 250 mM KCl at room temperature, crystallization of a epimerase/NADH/UDP-glucose ternary complex
-
hanging drop vapor diffusion method at 4°C, the crystal structures of WbpP in complex with cofactor and either UDP-Glc or UDP-GalNAc are determined at 2.5 and 2.1 A, respectively
sitting drop vapor diffusion method, using 29% (v/v) 2-ethoxyethanol and 0.1 M cacodylate buffer (pH 6.6), at 20°C
hanging drop vapor diffusion methodthree-dimensional structure of gal10p in complex with NAD+, UDP-glucose, and beta-D-galactose is determined to 1.85 A resolution. Space group I222 with unit cell dimensions of a = 120.9 A, b = 125.2 A and c = 142.3 A. The asymmetric unit contains one monomer
-
hanging drop vapor diffusion method, crystal structure of the enzyme (TMGalE) and the enzyme bound to UDP-glucose is determined at resolutions of 1.9 A and 2.0 A, respectively
purified recombinant unbound enzyme TMGalE, and TMGalE bound to UDP-Glc, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K153N
-
the mutation affects the catalytic activity only slightly, however, the NAD+ binding potential is reduced dramatically
K160V
site-directed mutagenesis of the key residue responsible for anchoring of the co-factor, inactive mutant
L320C
site-directed mutagenesis of a gate-keeper residue, the L320C mutant enzyme is also active in UDPGlcpNAc/UDP-GalpNAc interconversion
L320Y
site-directed mutagenesis of a gate-keeper residue, the L320Y mutant enzyme is not active in UDPGlcpNAc/UDP-GalpNAc interconversion
Y156F
site-directed mutagenesis of the key residue serving as the active site base, inactive mutant
N191D
K153A
-
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. 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
K153M
N179S
the 4-epimerization of tagatose is enhanced 2fold in this mutant
S124A
S124A/Y149F
S124T
S124V
S143A
site-directed mutagenesis, the mutation abolishes activity on non-acetylated substrates, probably due to loss of the hydrogen bonding, whereas the mutant remains active on UDP-GlcNAc/UDP-GalNAc, as additional stabilizing interactions with the N-acetyl moiety are present
S301Y
CCQ00728.1
mutation results in loss of UDP-GlcNAc/UDP-GalNAc conversion activity
S306Y
Y149F
Y299C
S301Y
-
mutation results in loss of UDP-GlcNAc/UDP-GalNAc conversion activity
-
S306Y
-
plasmid containing the Gne S306Y constructed using the QuikChange Site-Directed Mutagenesis kit (Stratagene, La Jolla, CA).The S306Y mutation totally abolished activity toward the acetylated substrate.
-
C307Y
-
normal activity with respect to UDP-galactose, complete loss of activity with respect to UDP-N-acetylgalactosamine
D103G
G302D
the mutant enzyme is not able to rescue galactose-sensitive cell proliferation when stably expressed in ldlD cells
G319E
-
very littel change in steady-state kinetic parameters compared with the wild-type protein
G90E
K257R
-
the ratio of turnover number to Km-value is 6.7fold lower than the wild-type ratio
L183P
L313M
-
the ratio of turnover number to Km-value is 3.0fold lower than the wild-type ratio
M284K
-
the mutant is active in vivo, but not in vitro and shows reduced enzymatic activity (1.1% residual activity) and reduced stability towards denaturants in vitro
N34S
R239W
the mutant enzyme is not able to rescue galactose-sensitive cell proliferation when stably expressed in ldlD cells
R335H
S132A
-
complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
S132A/Y157F
-
complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
V94M
Y157F
-
complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
G118A/G119A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
G188S/G119S
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S116A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
S279Y
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
T117S
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates
Y151A
the mutant enzyme is not well expressed. Purified Y151A AglW is inactive with all UDP-Hex/HexNAc compounds as well as with GlcNAc/GalNAc-PP-PhU as substrates
K150R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
K150R
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
-
A209H
the mutant is much less efficient in catalyzing the epimerization of N-acetylated hexose moieties and is more efficient in catalyzing the reaction for non-acetylated hexoses compared with wild-type
S306Y
mutant is completely inactive irrespective of the substrate tested
C300Y
site-directed mutagenesis, the mutation results in decreased activity toward UDP-GlcNAc and UDP-GalNAc
K86G
site-directed mutagenesis, the mutation abolishes the ability of the enzyme to transform UDP-Glc/UDP-Gal completely
C300Y
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
-
site-directed mutagenesis, the mutation results in decreased activity toward UDP-GlcNAc and UDP-GalNAc
-
K86G
Streptococcus pneumoniae ATCC BAA-334 / TIGR4
-
site-directed mutagenesis, the mutation abolishes the ability of the enzyme to transform UDP-Glc/UDP-Gal completely
-
additional information
N191D
naturally occuring mutation, the UgeA mutant shows reduced galactofuranose production, the mutant enzyme is partially active
N191D
Aspergillus niger CBS 513.88 / FGSC A1513
-
naturally occuring mutation, the UgeA mutant shows reduced galactofuranose production, the mutant enzyme is partially active
-
K153M
-
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. 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
K153M
mutation results in a 13C chemical shift of 150.8 ppm, which is 0.9 ppm downfield from that of wild-type and 1.8 ppm upfield from that of Y149F epimerase
K153M
-
site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme
S124A
-
mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively
S124A
decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations
S124A
-
in contrast to wild-type enzyme the mutant enzyme displays a significant deuterium kinetic isotope effect. Epimerization proceeds with a deuterium kinetic isotope effect of about 2 throughout the pH range 6.3-9.0
S124A
-
site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme
S124A/Y149F
mutation causes a 13C downfield perturbation of 2.8 ppm to 152.7 ppm
S124A/Y149F
-
epimerization proceeds at a turnover number that is lower by a factor of 10000000 than that of the wild-type enzyme. This is attributed to the synergistic action of Tyr149 and Ser124 in wild-type enzyme and to the absence of any internal catalysis of hydride transfer in the doubly mutated enzyme. 80% inactivation after 8 min at 50°C compared to 20% inactivation of the wild-type enzyme
S124T
-
mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively
S124T
decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations
S124T
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S124V
-
mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively
S124V
decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations
S306Y
-
plasmid containing the Gne S306Y constructed using the QuikChange Site-Directed Mutagenesis kit (Stratagene, La Jolla, CA).The S306Y mutation totally abolished activity toward the acetylated substrate.
S306Y
site-directed mutagenesis, the mutation allows a switch from group 2 to group 1 and forms steric clashes between the group 3 epimerases and their substrates,which results in the observed loss of activity
Y149F
-
mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values form Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively
Y149F
mutation results in a 13C downfield perturbation of 2.7 ppm to 152.6 ppm
Y149F
-
in contrast to wild-type enzyme the mutant enzyme displays a significant deuterium kinetic isotope effect. At pH there is no significant isotope effect, but at pH 6.3, the isotope effect is 2.2
Y149F
-
site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme
Y299C
-
mutation results in a loss of epimerase activity with regard to UDPgalactose by almost 5fold, it results in a gain of activity against UDP-GalNAc by more than 230fold
Y299C
site-directed mutagenesis, structure analysis in complex with UDP-N-acetylglucosamine, PDB ID 1LRK, the Y299C mutation in eGalE results in significant loss of activity on non-acetylated substrates
D103G
-
the ratio of turnover number to Km-value is 14.4fold lower than the wild-type ratio
G90E
-
the ratio of turnover number to Km-value is 1040fold lower than the wild-type ratio. Mutant enzyme is more susceptible to proteolysis than the wild-type protein, presence of substrate at saturating level (1 mM) partially protect the enzyme from proteolysis
L183P
-
the ratio of turnover number to Km-value is 4.7fold lower than the wild-type ratio. Mutant enzyme is highly susceptible to proteolysis during expression and purification
N34S
-
very little change in steady-state kinetic parameters compared with the wild-type protein. Mutant enzyme is more susceptible to proteolysis than the wild-type protein, presence of substrate at saturating level (1 mM) partially protect the enzyme from proteolysis
R335H
-
the ratio of turnover number to KM-value is 3.5fold lower than the wild-type ratio
V94M
-
the ratio of turnover number to Km-value is 75fold lower than the wild-type ratio
additional information
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides, phenotype, overview
additional information
-
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides, phenotype, overview
additional information
-
identification of a mutant allele of UDP-glucose epimerase 4 (UGE4)/root hair defective 1/root epidermal bulgar 1, which is a mutant with swollen root epidermal cells and has an altered sugar composition in cell wall polysaccharides, phenotype, overview
-
additional information
-
generation of single disruption mutants and DELTAuge3 DELTAuge5 double mutant, phenotypes, overview
additional information
-
generation of single disruption mutants and DELTAuge3 DELTAuge5 double mutant, phenotypes, overview
-
additional information
-
a ugeADELTA knockout strain is viable, but has defects including wide, slow growing, highly branched hyphae and reduced conidiation. ugeADELTA colonies have substantially reduced sporulation but normal spore viability. Conidia of the ugeADELTA strain can not form colonies on galactose as a sole carbon source, however they produced short, multinucleate germlings, suggesting they ceased to grow from starvation
additional information
targeted deletion of ugeA resulting in a severe reduction of galactofuranose in N-linked glucans
additional information
Aspergillus niger CBS 513.88 / FGSC A1513
-
targeted deletion of ugeA resulting in a severe reduction of galactofuranose in N-linked glucans
-
additional information
-
second-order rate constants for reductive inactivation of wild-type and mutant epimerases, overview
additional information
silencing gene GALE with specific siRNAs in human chondrocytes
additional information
-
silencing gene GALE with specific siRNAs in human chondrocytes
additional information
addition of NAD+ to Lys150 significantly abrogates the loss of activity. None of the mutations affected the quaternary structure of the protein
additional information
-
addition of NAD+ to Lys150 significantly abrogates the loss of activity. None of the mutations affected the quaternary structure of the protein
-
additional information
development of transgenic rice plants to constitutively overexpress the OsUGE-1 gene (OsUGE1-OX1-2). The transgenic rice lines are similar in size to wild-type plants at the vegetative stage and at maturity regardless of the N-level tested. OsUGE1-OX lines maintain 18-24% more sucrose and 12-22% less cellulose in shoots compared to wild-type when subjected to suboptimal N-levels. OsUGE1-OX lines maintain proportionally more galactose and glucose in the hemicellulosic polysaccharide profile of plants compared to wild-type plants when grown under low N. The altered cell wall C-partitioning during N-limitation in the OsUGE1-OX lines appears to be mediated by OsUGE1 via the repression of the cellulose synthesis associated genes, OsSus1, OsCesA4, 7, and 9. Seed characteristics of rice plants overexpressing OsUGE1 compared to wild-type rice, overview
additional information
a GalE loop deletion mutant (mut1), in which residues 32-43 (NLSSGRREFVNP) of the NAD-binding loop are replaced with residues 33-40 (IVQRDTGG) of the corresponding loop from Thermoplasma volcanium binds NAD+ in a loose, reversible manner
additional information
-
a GalE loop deletion mutant (mut1), in which residues 32-43 (NLSSGRREFVNP) of the NAD-binding loop are replaced with residues 33-40 (IVQRDTGG) of the corresponding loop from Thermoplasma volcanium binds NAD+ in a loose, reversible manner
additional information
construction of disruption mutants, DELTAuge1 and DELTAuge1DELTAgal10. Both mutant strains are sensitive to hygromycin B. Oligosaccharide content is reduced in acid phosphatase prepared from the uge1DELTA strain. The uge1DELTA strain grown in 0.1% glucose, 2% galactose medium shows a rise of UDP-glucose/-galactose epimerase activity while no detectable increase in activity is observed in the uge1Dgal10D strain. Gal10p can replace loss of Uge1p in the uge1DELTA mutant in glucose medium. Growth and galactosylation phenotypes of uge1DELTA, overview
additional information
-
construction of disruption mutants, DELTAuge1 and DELTAuge1DELTAgal10. Both mutant strains are sensitive to hygromycin B. Oligosaccharide content is reduced in acid phosphatase prepared from the uge1DELTA strain. The uge1DELTA strain grown in 0.1% glucose, 2% galactose medium shows a rise of UDP-glucose/-galactose epimerase activity while no detectable increase in activity is observed in the uge1Dgal10D strain. Gal10p can replace loss of Uge1p in the uge1DELTA mutant in glucose medium. Growth and galactosylation phenotypes of uge1DELTA, overview
additional information
-
construction of disruption mutants, DELTAuge1 and DELTAuge1DELTAgal10. Both mutant strains are sensitive to hygromycin B. Oligosaccharide content is reduced in acid phosphatase prepared from the uge1DELTA strain. The uge1DELTA strain grown in 0.1% glucose, 2% galactose medium shows a rise of UDP-glucose/-galactose epimerase activity while no detectable increase in activity is observed in the uge1Dgal10D strain. Gal10p can replace loss of Uge1p in the uge1DELTA mutant in glucose medium. Growth and galactosylation phenotypes of uge1DELTA, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
-
2 h, stable in presence of 1% bovine serum albumin, 0.5 mM dithiothreitol or 1 mM mercaptoethanol
25
30
37
40
41
Saccharomyces fragilis
-
2 min, desensitization by heat converts the enzyme to its ultimate catalytic form
42
45
50
60
70
80
90
30
-
53% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM
30
-
53% loss of activity within 10 min, partial protection by NAD+, up to a concentration of 7 mM
37
-
85% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM
37
-
85% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM. Partial protection by addition of NAD+ up to a concentration of 1 mM
40
recombinant Pisum enzyme loses both activities completely at temperatures higher than 40°C
50
-
wild-type enzyme loses 20% of its activity after 8 min, mutant enzyme S124A/Y149F loses 80% of its activity after 8 min
70
purified recombinant His6-tagged enzyme, no significant decrease in enzyme activity after 3 h
80
purified recombinant His6-tagged enzyme, retains more than 85% of its original activity under standard assay conditions after 3 h
90
purified recombinant His6-tagged enzyme, retains 50% of its original activity under standard assay conditions after 40 min
90
-
enzyme is stable at 90°C, after incubating at this temperature for 10 min, 90% of the enzymatic activity remains
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
uridine nucleotides provide almost total protection against the apparent first order inactivation of epimerase by trypsin. NAD+ partially protects against trypsin inactivation
-
when trypsinized in the presence of 2.5 mM 5'-UMP, the mutarotase activity is lost in a time-dependent manner without affecting the epimerase activity. Proteolysis under identical conditions in the presence of 6.7 mM galactose or fructose leads to reversal of this protection - epimerase activity is completely lost whereas mutarotase activity is 90% protected
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diethyldicarbonate
-
incubation of the recombinant His6-tagged protein with increasing concentrations of diethyldicarbonate (1.0-5.0 mM) results in a time-dependent loss of activity
Glycerol
-
the use of glycerol as a cosolvent enhances the GalE thermostability significantly. The enzyme in 50% glycerol can retain 90% of its activity, whereas only 20% activity is observed for the identically treated control enzyme
urea
-
denaturation by 8 M urea at pH 7.0 causes 85% loss of ist secondary structure and dissociation of its constituent molecules
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, dilute solutions of highly purified liver or mammary enzyme are very stable in the presence of 20 to 200 mM potassium phosphate, 20% glycerol, 1 mM mercaptoethanol, at pH 7.6, 10% loss of activity after 6 months
-
-20°C, pH 8, 25% glycerol or 20% adonitol in 20 mM Tris, enzyme can be kept active without any significant loss of activity
4°C or -20°C, 0.2 mg/ml enzyme concentration, 0.01 M potassium phosphate buffer, pH 7.5. About 60% of the initial activity remains for 3 months at 4°C without any protector, and in the presence of 20% glycerol more than 80% of the activity remains
-
4°C, dilute solutions of highly purified liver or mammary enzyme are very stable in the presence of 20 to 200 mM potassium phosphate, 20% glycerol, 1 mM mercaptoethanol, at pH 7.6
-
stable for several months if mixed with an equal volume of glycerol and stored in liquid nitrogen
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration
Q81JK4, Q81K34
DEAE-Toyopearl column chromatography and Superdex 200 gel filtration
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
-
purification of the native enzyme from pea sprouts by ion exchange chromatography and gel filtration, further purification on a hydroxyapatite column, purification of recombinant enzymes by ion exchange chromatography
purification of the recombinant Arabidopsis enzyme by Ni-NTA affinity chromatography
purification of the recombinant enzyme by Ni-NTA affinity chromatography
recombinant enzyme
recombinant fusion enzyme 2.33fold from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, native UGE1 334fold from sprouts by ammonium sulfate fractionation and a chromatographic procedure
recombinant His-tagged enzyme by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His6-tagged isozymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21-Gold (DE3)
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-Gold by nickel affinity chromatography and ultrafiltration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, quantitative real-time reverse transcription PCR enzyme expression analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli Rosetta cells and in a gal10-null strain of Saccharomyces cerevisiae strain JFy3835
-
expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in GALE-null line of Chineses hamster ovary cells. GALE-null cells accumulats abnormally high levels of Hal-1-P and UDP-Gal and abnormally low levels of UDP-Glc and UDP-GLcNAc in the presence of galactose. Human GALE expression corrects each of theses defects
-
expression in GALE-null line of Chinesese hamster ovary cells. Enzyme from Escherichia coli can not restore the metabolic balance, because unlike the mammalian enzyme it can not catalyze the interconversion of UDP-GalNAc and UDP-GlcNAc
-
expression of GFP-tagged wild-type enzyme in HEK-293T cells, and transient expression of myc-tagged GALER239W and GALEG302D, and of myc- or FLAG-tagged GALE165K and GALEW336X in HEK-293T cells and in GALE-null ldlD cells
expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Gold
expression of the enzyme obtained from HB8 strain in Escherichia coli as His-tagged protein
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
-
galE transcription exhibits a distinct expressionprofile under different culture conditions, mapping of galE transcription initiation
-
gene BAS5114, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
Q81JK4, Q81K34
gene fnlA or ABD1_580, DNA and amino acid sequence determination and analysis, sequence comparisons, the gene belongs to the components of polysaccharide biosynthesis cluster RGP01, overview, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
gene galE, functional expression of N-termminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene GALE, real-time quantitative PCR expression analysis in chondrocytes
gene galE, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression in and functional complementation of enzyme-deficient Escherichia coli strain BW25113 DELTAgalE
gene galE-1, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene galE1 or Rv3634c, sequence comparisons, e.g. with the enzyme from Mycobacterium smegmatis strain mc2 4517, recombinant expression of His-tagged enzyme in Escherichia coli strains BL21(DE3)pLysS, BL21(DE3), BL21-CodonPlus(DE3)-RIPL, OverExpress C41(DE3), or OverExpress C43(DE3)pLysS, and recombinant expression of the enzyme in Mycobacterium smegmatis strain mc2 4517, none of these approaches leads to expression of the enzyme in the soluble form, except for strain BL21(DE3)pLysS, recombinant expression of enzyme mutants
gene galEsp2 or galE-2, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene OsUGE-1, phylogenetic analysis of the UGEs from Oryza sativa, recombinant overexpression in Oryza sativa via Agrobacterium tumefaciens-mediated transformation, real-time PCR enzyme expression analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene UGE1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of the enzyme fused to thioredoxin and His6 in Escherichia coli strain BL21(DE3)
gene uge1, is constitutively expressed, recombinant expression in Escherichia coli strain XL-1 blue
gene UGE1, transcriptome-guided search by transcriptome analysis of Ornithogalum caudatum unigenes, cloning, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of soluble His-tagged N-terminally truncated enzyme in Escherichia coli strain
gene UGE2, transcriptome-guided search by transcriptome analysis of Ornithogalum caudatum unigenes, cloning, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of soluble His-tagged N-terminally truncated enzyme in Escherichia coli strain Transetta (DE3)
gene ugeA, DNA and amino acid sequence determination and analysis, cytoplasmic expression of GFP-tagged UgeA in Aspergillus nidulans from a plasmid under control of the wild-type promoter, expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli
-
genes uge3 and uge5, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3), expression as fluorescence labeled proteins uge3-gfp and uge5-rfp in Aspergillus. fumigatus strain Af293
-
mutant enzymes S132A, Y157F, S132A/Y157F and C307Y are expressed in a null-background strain of Saccharomyces cerevisiae. S132a/Y157F and C307Y are also overexpressed in Pichia pastoris
-
recombinant enzyme overexpression in Thermus thermophilus strain HB27 to an increased capacity of biofilm production, expression of His-tagged enzyme
-
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21-Gold (DE3)
recombinant protein is expressed in Escherichia coli with C-terminal His-tag
To explore the quantitative relationship between GALE activity and galactose metabolism and sensitivity in yeast, a strain is generated in which the expression of GAL10, encoding GALE, was regulated by doxycycline. In brief, a doxycycline-repressible promoter is introduced just upstream of the GAL10 coding sequence in a strain (JFy4763) that was otherwise wild type for all Leloir pathway enzymes and that was engineered to express the appropriate doxycycline-responsive transcriptional activator and repressor protein moieties.
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GALE mRNA expression is stimulated by interleukin-1beta in early phase, but suppressed in late phase, while the suppression of GALE expression induced by interleukin-1beta is mainly mediated by stress-activated protein kinase/c-Jun N-terminal kinase pathway
GALE mRNA expression is stimulated by interleukin-1beta in early phase, but suppressed in late phase, while the suppression of GALE expression induced by interleukin-1beta is mainly mediated by stress-activated protein kinase/c-Jun N-terminal kinase pathway. Both SAP/JNK inhibitor SP600125 and p38 MAPK inhibitor SB203580 attenuate the suppression of interleukin-1beta on GAG synthesis and GALE mRNA expression of chondrocyte
gene galE is positively regulatedby Clp and RpfF
gene galE is subject to catabolite repression
overexpression in Thermus thermophilus HB27 leads to an increased capacity of biofilm production
-
the expression level of OsUGE2 is significantly reduced in the Osfc24 mutant compared with the wild-type
uge1 is not induced by glucose
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation in presence of 8 M urea. Dilution of the denaturant by sodium phosphate buffer, 20 mM, pH 7.0, containing 1 mM NAD+ recovers the activity to the extent of 80-100%
-
denatured by 8 M urea at pH 7.0 to a state having 15% of residual secondary structure. Dilution of the denaturant by 20 mM potassium phosphate, pH 8.5, leads to functional reconstitution of the enzyme. Reactivation follows a socond-order kinetics
-
dilution of the denaturant urea by buffer at pH 8.5 leads to functional reconstitution of the dimeric holoenzyme. The refolding process is biphasic: after 2 min an equilibrium conformer is formed having 72% of its native secondary structure and by 60 min reactivation becomes complete. The early intermediate has lower energy of activation against thermal denaturation than the reactivated state
-
purified enzyme dimer consists of a mixture of catalytically active subunits designated enzyme-NAD+ and inactive, abortive complexes designated enzyme-NADH-uridine nucleotide, in which the uridine nucleotide may be UDPglucose, UDPgalactose, or UDP. The abortive complexes are transformed into active enzyme-NAD+ by denaturation of the purified enzyme at 4°C in 6 M guanidine hydrochloride buffered at pH 7.0 in the presence of 0.126 mM NAD+ for 3 h, followed by dilution of guanidine hydrochloride to 0.18 M and of NAD+ to 0.076 mM for 2 h. The renatured enzyme is fully active and contains negligible amounts of NADH and uridine nucleotides
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
possible use of this enzyme as a biomarker for well and moderately differentiated tumors
medicine
synthesis
medicine
-
The absence of CaGAL10 alone does not significantly reduce virulence in mouse model studies, but since it leads to increased drug sensitivity, it can be explored as a potential drug target in combination with other candidacidal drugs. Thus the UDP-galactose-4-epimerase plays an important role in the biology of the human pathogen, Candida albicans, like in the case of several other pathogens.
medicine
-
Trypanosoma brucei GalE is a validated drug target for African sleeping sickness. The Trypanosoma brucei enzyme can be selectively inhibited by small molecules that are not substrate analogues in vitro, although the mechanism of cytotoxicity of these inhibitors is unconfirmed. Of the compounds screened, ethacrynic acid displays the best therapeutic index, but is clinically used as a loop diuretic and was found to form multiple covalent adducts with TbGalE in vitro, limiting its potential as a lead compound.
medicine
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Galactosylation of one or more glycoprotein(s), most likely in the endosomal/lysosomal system, is essential for the survival of bloodstream form Trypanosoma brucei. GalE-encoded epimerase and the downstream UDP-Gal transporters and UDP-Gal-dependent glycosyltransferases may be exploitable as drug targets.
medicine
SjGALE is a potential vaccine against Schistosoma japonicum
medicine
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Hericium erinaceus is an important medicinal fungus in traditional Chinese medicine because of its polysaccharides and other natural products. When A6180 is introduced into Saccharomyces cerevisiae BY4742, xylose is detected in the polysaccharide composition of the yeast transformant. The generated polysaccharides with a new composition of sugars show enhanced macrophage activity in vitro. The enzyme (A6180) plays an important role in the structure and activity of polysaccharides. It is a promising strategy for producing polysaccharides with higher activity by introducing A6180 into polysaccharide-producing mushrooms
medicine
-
Hericium erinaceus is an important medicinal fungus in traditional Chinese medicine because of its polysaccharides and other natural products. When A6180 is introduced into Saccharomyces cerevisiae BY4742, xylose is detected in the polysaccharide composition of the yeast transformant. The generated polysaccharides with a new composition of sugars show enhanced macrophage activity in vitro. The enzyme (A6180) plays an important role in the structure and activity of polysaccharides. It is a promising strategy for producing polysaccharides with higher activity by introducing A6180 into polysaccharide-producing mushrooms
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synthesis
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preparation of a fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker, shows kinetic advantages in that the initial velocity to produce glucose 1-phosphate from UDPgalactose an
synthesis
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the enzyme is a valuable biocatalyst for the synthesis of UDP-galactose from UDP-glucose
EXTERNAL LINKS (specific for EC-Number 5.1.3.2)
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Release 2026.1 (March 2026)
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