Information on EC 5.1.3.2 - UDP-glucose 4-epimerase and Organism(s) Homo sapiens

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Homo sapiens


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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
5.1.3.2
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RECOMMENDED NAME
GeneOntology No.
UDP-glucose 4-epimerase
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
colanic acid building blocks biosynthesis
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D-galactose degradation I (Leloir pathway)
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D-galactose degradation V (Leloir pathway)
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D-galactose detoxification
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mycolyl-arabinogalactan-peptidoglycan complex biosynthesis
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stachyose degradation
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superpathway of UDP-glucose-derived O-antigen building blocks biosynthesis
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UDP-alpha-D-galactose biosynthesis
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degradation of hexoses
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Galactose metabolism
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Amino sugar and nucleotide sugar metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-89-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
UDP-galactose
UDP-glucose
show the reaction diagram
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
UDP-GlcNAc
UDP-GalNAc
show the reaction diagram
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-
-
r
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
UDP-galactose
UDP-glucose
show the reaction diagram
UDP-GalNAc
UDP-GlcNAc
show the reaction diagram
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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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r
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diamino(dimethylamino)methyl (E)-{(8alpha,13E,14alpha)-14-[2-(furan-3-yl)ethyl]-8-methylpodocarpan-13-ylidene}methyl sulfate
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diethylstilbestrol
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ebselen
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Ethacrynic acid
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haloprogin
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psammaplin A
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035 - 0.38
UDP-galactose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046 - 36
UDP-galactose
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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75
diethylstilbestrol
Homo sapiens;
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0.014
ebselen
Homo sapiens;
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14
Ethacrynic acid
Homo sapiens;
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0.5
haloprogin
Homo sapiens;
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3.6
psammaplin A
Homo sapiens;
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38266
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x * 38266, calculation from nucleotide sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 38266, calculation from nucleotide sequence
dimer
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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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization of the epimerase/UDP-GLcNAc/NADH abortive complex
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suitable crystallization conditions are both at room temperature and at 4C 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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel agarose column chromatography
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recombinant enzyme
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recombinant wild-type and mutant enzymes S132A, Y157F, S132A/Y157F and C307Y
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta cells and in a gal10-null strain of Saccharomyces cerevisiae strain JFy3835
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expression in Escherichia coli
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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
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expression in Pichia pastoris
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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
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A25V
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the mutant shows reduced activity compared to the wild-type enzyme
C307Y
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normal activity with respect to UDP-galactose, complete loss of activity with respect to UDP-N-acetylgalactosamine
D69E
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the mutant shows reduced activity compared to the wild-type enzyme
E165K
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unstable mutant
G302D
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the mutant enzyme is not able to rescue galactose-sensitive cell proliferation when stably expressed in ldlD cells
G319E
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very littel change in steady-state kinetic parameters compared with the wild-type protein
K257R
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the ratio of turnover number to Km-value is 6.7fold lower than the wild-type ratio
L313M
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the ratio of turnover number to Km-value is 3.0fold lower than the wild-type ratio
M284K
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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
N268D
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the mutant demonstrates 63% residual activity
R169W
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the mutant shows reduced activity compared to the wild-type enzyme
R239W
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the mutant enzyme is not able to rescue galactose-sensitive cell proliferation when stably expressed in ldlD cells
R40C
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the mutant shows reduced activity compared to the wild-type enzyme
S132A
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complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
S132A/Y157F
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complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc
W336X
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unstable mutant
Y105C
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the mutant demonstrates 13% residual activity
Y157F
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complete loss of activity with respect to interconversion of UDP-glucose and UDP-galactose and of UDP-GalNAc and UDP-GlcNAc