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Information on EC 5.1.3.2 - UDP-glucose 4-epimerase and Organism(s) Escherichia coli and UniProt Accession P09147

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     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.
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Select one or more organisms in this record:
This record set is specific for:
Escherichia coli
UNIPROT: P09147
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Escherichia coli
Synonyms
4-Epimerase, 6xHis-rGalE, An14g03820, AtUGE1, AtUGE2, AtUGE3, AtUGE4, AtUGE5, CaGAL10, CapD, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-Epimerase
-
-
-
-
Epimerase, uridine diphosphoglucose
-
-
-
-
Galactowaldenase
-
-
-
-
UDP-D-galactose 4-epimerase
-
-
-
-
UDP-Gal 4-epimerase
296155
-
UDP-galactose 4'-epimerase
246
-
UDP-galactose 4-epimerase
UDP-galactose-4-epimerase
294714
-
UDP-GlcNAc/Glc 4-epimerase
246
-
UDP-glucose epimerase
-
-
-
-
UDP-hexose 4-epimerase
UDP-sugar 4-epimerase
296155
-
UDPG-4-epimerase
-
-
-
-
UDPgalactose 4-epimerase
-
-
-
-
Uridine diphosphate galactose 4-epimerase
Uridine diphosphate glucose 4-epimerase
-
-
-
-
Uridine diphospho-galactose-4-epimerase
-
-
-
-
Uridine diphosphogalactose-4-epimerase
294714
-
Uridine diphosphoglucose 4-epimerase
-
-
-
-
Uridine diphosphoglucose epimerase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose = UDP-alpha-D-galactose
show the reaction diagram
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
B1X789
-
additional information
-
catalyses the interconversion of UDP-Gal and UDPGlc
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-89-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
-
-
-
-
r
ADP-D-glucose
?
show the reaction diagram
-
-
-
-
-
CDP-D-glucose
?
show the reaction diagram
-
-
-
-
-
D-fructose
D-tagatose
show the reaction diagram
B1X789
-
-
-
?
D-galactose
D-glucose
show the reaction diagram
B1X789
the catalytic efficiencies of GalE for D-galactose is much lower than for UDP-galactose
-
-
?
D-glucose
D-galactose
show the reaction diagram
B1X789
-
-
-
?
D-psicose
D-sorbose
show the reaction diagram
B1X789
-
-
-
?
D-sorbose
D-psicose
show the reaction diagram
B1X789
-
-
-
?
D-tagatose
D-fructose
show the reaction diagram
B1X789
the catalytic efficiencies of GalE for D-tagatose is much lower than for UDP-galactose
-
-
?
Deoxy-UDP-D-glucose
?
show the reaction diagram
-
-
-
-
-
TDP-6-deoxy-D-galactose
?
show the reaction diagram
-
-
-
-
-
TDP-D-glucose
TDP-D-galactose
show the reaction diagram
UDP-6-deoxy-D-glucose
?
show the reaction diagram
-
-
-
-
-
UDP-6-deoxygalactose
UDP-6-deoxyglucose
show the reaction diagram
-
-
-
-
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
UDP-D-fucose
?
show the reaction diagram
-
-
-
-
-
UDP-D-galactose-hexodialose
?
show the reaction diagram
-
-
-
-
-
UDP-D-xylose
?
show the reaction diagram
-
-
-
-
-
UDP-galactose
UDP-glucose
show the reaction diagram
UDP-Glc
UDP-Gal
show the reaction diagram
-
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
UDP-L-arabinose
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
-
-
-
-
?
UDP-galactose
UDP-glucose
show the reaction diagram
UDP-Glc
UDP-Gal
show the reaction diagram
-
-
-
-
r
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
contains none of the common metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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-(adenosine-5'-diphosphoryl)-D-ribose
-
reductive inhibition
5-(thymidine-5'-diphosphoryl)-D-glucose
-
reductive inhibition
5-(Thymidine-5'-diphosphoryl)-D-ribose
-
reductive inhibition
Glucose plus UMP
-
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
-
NaBH4
-
reductive inhibition
P1-5'-Uridine-P2-glucose-6-yl diphosphate
-
-
Sodium cyanoborohydride
-
NAD+ associated with the wild type enzyme is subject to UMP-dependent reduction, mutant proteins K153M and K153A bind UMP very well, but the rate at which NAD+ associated with them is reduced by sodium cyanoborohydride is almost insensitive to the presence of UMP
Thymidine diphospho-6-deoxy-D-xylo-4-hexosulose
-
reductive inhibition
-
UDP-6-deoxygalactose
-
weak competitive inhibitor with respect to UDPgalactose
Uridine 5'-diphosphate bromoacetol
-
-
Uridine 5'-diphosphate chloroacetol
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uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
powerful competitive
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UDP
-
activates the reduction of epimerase-bound NAD+
UMP
-
activates the reduction of epimerase-bound NAD+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26.4
D-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35°C
2 - 37
D-tagatose
B1X789
in McIlvaine buffer (pH 7.5), at 35°C
2 - 260
UDP-alpha-D-glucose
0.295
UDP-Gal
-
-
0.16 - 0.255
UDP-galactose
0.373
UDP-GalNAc
-
-
0.37
UDP-Glc
-
-
0.323
UDP-GlcNAc
-
-
1.2
UDP-glucose
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24°C, pH 7.0
0.026 - 0.256
UDPgalactose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00026
D-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35°C
0.00545
D-tagatose
B1X789
in McIlvaine buffer (pH 7.5), at 35°C
0.073 - 760
UDP-alpha-D-glucose
500 - 750
UDP-galactose
18
UDP-glucose
-
24°C, pH 7.0
0.073 - 960
UDPgalactose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000097
D-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35°C
0.000023
D-tagatose
B1X789
in McIlvaine buffer (pH 7.5), at 35°C
2.9 - 3400
UDP-alpha-D-glucose
3333
UDP-galactose
B1X789
in McIlvaine buffer (pH 7.5), at 35°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
uridine-5'-diphosphoro-beta-1-(5-sulfonic acid)naphthylamidate
-
pH 8.8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.3
-
activity of the wild-type enzyme is pH-independent in the pH-range of 5.5-9.3
7.5
B1X789
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH-dependencies of wild-type and mutant enzymes, overview
6.4 - 9.6
-
6.4: 68% loss of maximal activity, 9.6: 79% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
B1X789
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
metabolism
-
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
physiological function
-
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures, such as capsular polysaccharide (CPS)
physiological function
-
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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
-
-
-
-
-
-
-
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
2 * 38000, SDS-PAGE
38800
-
gel filtration
39000
40000
79000
80000
160000
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker, dimeric form, gel filtration
320000
-
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker, tetrameric form, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40000, SDS-PAGE
dimer
monomer
tetramer
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
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S124A
-
site-directed mutagenesis
S124A/Y229F
-
site-directed mutagenesis, inactive mutant
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
S144K
-
site-directed mutagenesis, inactive mutant
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
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
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
B1X789
the 4-epimerization of tagatose is enhanced 2fold in this mutant
S124A
S124A/Y149F
S124T
S124V
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.
Y149F
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
additional information
-
second-order rate constants for reductive inactivation of wild-type and mutant epimerases, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
-
stable, monomeric and dimeric form
2342
8.5
-
25°C, 24 h, stable
2343
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
pH 8.5, 24 h, stable
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
urea
-
denaturation by 8 M urea at pH 7.0 causes 85% loss of ist secondary structure and dissociation of its constituent molecules
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
-
Ni+ affinity column chromatography
B1X789
recombinant enzyme
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli ER2566 cells
B1X789
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 in Saccharomyces cerevisiae EBY100.
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fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-phosphate uridylyltransferase with an intervening Ala3 linker
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arabshahi, A.; Flentke, G.R.; Frey, P.A.
Uridine diphosphate galactose 4-epimerase. pH-Dependence of the reduction of NAD+ by a substrate analog
J. Biol. Chem.
263
2638-2643
1988
Escherichia coli
Manually annotated by BRENDA team
Blackburn, P.; Ferdinand, W.
The concerted inactivation of Escherichia coli uridine diphosphate galactose 4-epimerase by sugar nucleotide together with a free sugar
Biochem. J.
155
225-229
1976
Escherichia coli
Manually annotated by BRENDA team
Gabrial, O.; Kalckar, H.M.; Darrow, R.A.
UDP-galactose-4-epimerase
ubunit enzymes: biochemistry and function (Ebner, K. B., ed.)
2
85-135
1975
Bos taurus, Escherichia coli, Kluyveromyces marxianus, Saccharomyces fragilis, Torulopsis candida, Vigna radiata var. radiata
-
Manually annotated by BRENDA team
Adair, W.L.; Gabriel, O.; Ullrey, D.; Kalckar, H.M.
4-Uloses as intermediates in enzyme-nicotinamide adenine dinucleotide-mediated oxidoreductase mechanisms
J. Biol. Chem.
248
4635-4639
1973
Escherichia coli
Manually annotated by BRENDA team
Spencer, M.; Blackburn, P.; Ferdinand, W.; Blackburn, G.M.
Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli uridine diphosphate galactose 4-epimerase
Biochem. J.
131
421-423
1973
Escherichia coli
Manually annotated by BRENDA team
Wilson, D.B.; Hogness, D.S.
The enzymes of the galactose operon in Escherichia coli. I. Purification and characterization of uridine diphosphogalactose 4-epimerase
J. Biol. Chem.
239
2469-2481
1964
Escherichia coli
Manually annotated by BRENDA team
Vorgias, C.E.; Lemaire, H.G.; Wilson, K.S.
Overexpression and purification of the galactose operon enzymes from Escherichia coli
Protein Expr. Purif.
2
330-338
1991
Escherichia coli
Manually annotated by BRENDA team
Bauer, A.J.; Rayment, I.; Frey, P.A.; Holden, H.M.
The isolation, purification, and preliminary crystallographic characterization of UDP-galactose-4-epimerase from Escherichia coli
Proteins Struct. Funct. Genet.
9
135-142
1991
Escherichia coli
Manually annotated by BRENDA team
Vanhooke, J.L.; Frey, P.A.
Characterization and activation of naturally occuring abortive complexes of UDP-galactose 4-epimerase from Escherichia coli
J. Biol. Chem.
269
31596-31504
1994
Escherichia coli
-
Manually annotated by BRENDA team
Tamada, Y.; Swanson, B.A.; Arabshahi, A.; Frey, P.A.
Preparation and characterization of a bifunctional fusion enzyme composed of UDP-galactose 4-epimerase and galactose-1-P uridylyltransferase
Bioconjug. Chem.
5
660-665
1994
Escherichia coli
Manually annotated by BRENDA team
Liu, Y.; Vanhooke, J.L.; Frey, P.A.
UDP-galactose 4-epimerase: NAD+ content and a charge-transfer band associated with the substrate-induced conformational transition
Biochemistry
35
7615-7620
1996
Escherichia coli
Manually annotated by BRENDA team
Liu, Y.; Thoden, J.B.; Kim, J.; Berger, E.; Gulick, A.M.; Ruzicka, F.J.; Holden, H.M.; Frey, P.A.
Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli
Biochemistry
36
10675-10684
1997
Escherichia coli
Manually annotated by BRENDA team
Nayar, S.; Bhattacharyya, D.
UDP-galactose 4-epimerase from Escherichia coli: existence of a catalytic monomer
FEBS Lett.
409
449-451
1997
Escherichia coli
Manually annotated by BRENDA team
Dutta, S.; Maiti, N.R.; Bhattacharyya, D.
Reversible folding of UDP-galactose 4-epimerase from Escherichia coli
Eur. J. Biochem.
244
407-413
1997
Escherichia coli
Manually annotated by BRENDA team
Flentke, G.R.; Frey, P.A.
Reaction of uridine diphosphate galactose 4-epimerase with a suicide inactivator
Biochemistry
29
2430-2436
1990
Escherichia coli
Manually annotated by BRENDA team
Thoden, J.B.; Gulick, A.M.; Holden, H.M.
Molecular structures of the S124A, S124T, and S124V site-directed mutants of UDP-galactose 4-epimerase from Escherichia coli
Biochemistry
36
10685-10695
1997
Escherichia coli, Escherichia coli (P09147)
Manually annotated by BRENDA team
Thoden, J.B.; Frey, P.A.; Holden, H.M.
High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol
Protein Sci.
5
2149-2161
1996
Escherichia coli
Manually annotated by BRENDA team
Thoden, J.B.; Frey, P.A.; Holden, H.M.
Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: implications for the catalytic mechanism
Biochemistry
35
5137-5144
1996
Escherichia coli, Escherichia coli (P09147)
Manually annotated by BRENDA team
Thoden, J.B.; Frey, P.A.; Holden, H.M.
Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli
Biochemistry
35
2557-2566
1996
Escherichia coli, Escherichia coli (P09147)
Manually annotated by BRENDA team
Swanson, B.A.; Frey, P.A.
Identification of lysine 153 as a functionally important residue in UDP-galactose 4-epimerase from Escherichia coli
Biochemistry
32
13231-13236
1993
Escherichia coli
Manually annotated by BRENDA team
Bauer, A.J.; Rayment, I.; Frey, P.A.; Holden, H.M.
The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 A resolution
Proteins
12
372-381
1992
Escherichia coli
Manually annotated by BRENDA team
Barat, B.; Bhattacharyya, D.
UDP-galactose 4-epimerase from Escherichia coli: formation of catalytic site during reversible folding
Arch. Biochem. Biophys.
391
188-196
2001
Escherichia coli
Manually annotated by BRENDA team
Wei, Y.; Lin, J.; Frey, P.A.
13C NMR analysis of electrostatic interactions between NAD+ and active site residues of UDP-galactose 4-epimerase: implications for the activation induced by uridine nucleotides
Biochemistry
40
11279-11287
2001
Escherichia coli (P09147)
Manually annotated by BRENDA team
Berger, E.; Arabshahi, A.; Wei, Y.; Schilling, J.F.; Frey, P.A.
Acid-base catalysis by UDP-galactose 4-epimerase: correlations of kinetically measured acid dissociation constants with thermodynamic values for tyrosine 149
Biochemistry
40
6699-6705
2001
Escherichia coli
Manually annotated by BRENDA team
Liu, Y.; Arabshahi, A.; Frey, P.A.
Rate enhancements brought about by uridine nucleotides in the reduction of NAD+ at the active site of UDP-galactose 4-epimerase
Bioorg. Chem.
28
29-37
2000
Escherichia coli
-
Manually annotated by BRENDA team
Chen, X.; Kowal, P.; Hamad, S.; Fan, H.; Wang, P.G.
Cloning, expression and characterization of a UDP-galactose 4-epimerase from Escherichia coli
Biotechnol. Lett.
21
1131-1135
1999
Escherichia coli
-
Manually annotated by BRENDA team
Bhattacharyya, U.; Dhar, G.; Bhaduri, A.
An arginine residue is essential for stretching and binding of the substrate on UDP-glucose-4-epimerase from Escherichia coli. Use of a stacked and quenched uridine nucleotide fluorophore as probe
J. Biol. Chem.
274
14573-14578
1999
Escherichia coli
Manually annotated by BRENDA team
Holden, H.M.; Rayment, I.; Thoden, J.B.
Structure and function of enzymes of the Leloir pathway for galactose metabolism
J. Biol. Chem.
278
43885-43888
2003
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Schulz, J.M.; Ross, K.L.; Malmstrom, K.; Krieger, M.; Fridovich-Keil, J.L.
Mediators of galactose sensitivity in UDP-galactose 4'-epimerase-impaired mammalian cells
J. Biol. Chem.
280
13493-13502
2005
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Guo, H.; Yi, W.; Li, L.; Wang, P.G.
Three UDP-hexose 4-epimerases with overlapping substrate specificity coexist in E. coli O86:B7
Biochem. Biophys. Res. Commun.
356
604-609
2007
Escherichia coli
Manually annotated by BRENDA team
Guo, H.; Li, L.; Wang, P.G.
Biochemical characterization of UDP-GlcNAc/Glc 4-epimerase from Escherichia coli O86:B7
Biochemistry
45
13760-13768
2006
Escherichia coli, Escherichia coli O86:B7
Manually annotated by BRENDA team
Zhang, H.C.; Bi, J.Y.; Chen, C.; Huang, G.L.; Qi, Q.S.; Xiao, M.; Wang, P.G.
Immobilization of UDP-galactose 4-epimerase from Escherichia coli on the yeast cell surface
Biosci. Biotechnol. Biochem.
70
2303-2306
2006
Escherichia coli
Manually annotated by BRENDA team
Kim, H.J.; Kang, S.Y.; Park, J.J.; Kim, P.
Novel activity of UDP-galactose-4-epimerase for free monosaccharide and activity improvement by active site-saturation mutagenesis
Appl. Biochem. Biotechnol.
163
444-451
2011
Escherichia coli (B1X789), Escherichia coli
Manually annotated by BRENDA team
Frey, P.A.; Hegeman, A.D.
Chemical and stereochemical actions of UDP-galactose 4-epimerase
Acc. Chem. Res.
46
1417-1426
2013
Escherichia coli
Manually annotated by BRENDA team
Beerens, K.; Soetaert, W.; Desmet, T.
UDP-hexose 4-epimerases a view on structure, mechanism and substrate specificity
Carbohydr. Res.
414
8-14
2015
Drosophila melanogaster (Q9W0P5), Escherichia coli (P09147), Homo sapiens, Homo sapiens (Q14376), Marinithermus hydrothermalis (F2NQX6), Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1 (F2NQX6), Saccharomyces cerevisiae (P04397), Saccharomyces cerevisiae ATCC 204508 / S288c (P04397), Streptococcus thermophilus (P21977), Thermus thermophilus (F6DEY6), Thermus thermophilus SG0.5JP17-16 (F6DEY6)
Manually annotated by BRENDA team
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