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5.1.3.2: UDP-glucose 4-epimerase

This is an abbreviated version!
For detailed information about UDP-glucose 4-epimerase, go to the full flat file.

Word Map on EC 5.1.3.2

Reaction

UDP-alpha-D-glucose
=
UDP-alpha-D-galactose

Synonyms

4-Epimerase, 6xHis-rGalE, ABD1_580, An14g03820, AtUGE1, AtUGE2, AtUGE3, AtUGE4, AtUGE5, CaGAL10, CapD, epimerase Ab-WbjB, Epimerase, uridine diphosphoglucose, fnlA, GAL10, Gal10p, Galactowaldenase, GalE, galE-1, galE-2, galE1, GalESp1, GalESp2, GNE, GNE2, H3634, HvUGE1, HvUGE2, HvUGE3, MdUGE1, More, OsUGE-1, OsUGE1, PsUGE1, Rdh1, rGalE, Rv3634c, TbGalE, TM0509, TMGalE, UDP-D-galactose 4-epimerase, UDP-D-glucose/UDP-D-galactose 4-epimerase, UDP-Gal 4-epimerase, UDP-Gal/Glc 4-epimerase, UDP-galactose 4'-epimerase, UDP-galactose 4-epimerase, UDP-galactose-4'-epimerase, UDP-galactose-4-epimerase, UDP-Glc 4-epimerase, UDP-Glc(NAc) 4-epimerase, UDP-GlcNAc 4-epimerase, UDP-GlcNAc/Glc 4-epimerase, UDP-glucose 4'-epimerase, UDP-glucose 4-epimerase, UDP-glucose 4-epimerase 1, UDP-glucose 4-epimerase 4, UDP-glucose epimerase, UDP-glucose-4-epimerase, UDP-glucose/-galactose 4-epimerase, UDP-hexose 4-epimerase, UDP-N-acetyl-glucosamine 4,6-dehydratase, UDP-sugar 4-epimerase, UDP-Xyl 4-epimerase, UDP-xylose 4-epimerase, UDPG-4-epimerase, UDPgalactose 4-epimerase, UGE, UGE-1, UGE1, UGE1:GUS, Uge1p, UGE2, UGE3, UGE3:GUS, UGE4, UGE5, UgeA, Uridine diphosphate galactose 4-epimerase, Uridine diphosphate glucose 4-epimerase, uridine diphosphate-galactose-4'-epimerase, Uridine diphospho-galactose-4-epimerase, Uridine diphosphogalactose-4-epimerase, Uridine diphosphoglucose 4-epimerase, Uridine diphosphoglucose epimerase, uridine-diphospho-glucose 4-epimerase, WbjB

ECTree

     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.2 UDP-glucose 4-epimerase

Engineering

Engineering on EC 5.1.3.2 - UDP-glucose 4-epimerase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M134A
site-directed mutagenesis
M134Y
site-directed mutagenesis
M134A
-
site-directed mutagenesis
-
M134Y
-
site-directed mutagenesis
-
K153N
-
the mutation affects the catalytic activity only slightly, however, the NAD+ binding potential is reduced dramatically
Y149G
-
the mutant is completely inactive
Y149G/K153N
-
the mutant is completely inactive
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
S124A/Y229F
site-directed mutagenesis, inactive mutant
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
S144K
site-directed mutagenesis, inactive mutant
S306Y
Y149F
Y299C
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.
-
A25V
the mutant shows reduced activity compared to the wild-type enzyme
C307Y
-
normal activity with respect to UDP-galactose, complete loss of activity with respect to UDP-N-acetylgalactosamine
D103G
D69E
the mutant shows reduced activity compared to the wild-type enzyme
E165K
unstable mutant
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
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
N268D
-
the mutant demonstrates 63% residual activity
R169W
the mutant shows reduced activity compared to the wild-type enzyme
R239W
the mutant enzyme is not able to rescue galactose-sensitive cell proliferation when stably expressed in ldlD cells
R335H
R40C
the mutant shows reduced activity compared to the wild-type enzyme
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
W336X
unstable mutant
Y105C
-
the mutant demonstrates 13% residual activity
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
K150R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
S121A
site-directed mutagenesis, inactive mutant
Y146F
site-directed mutagenesis, inactive mutant
K150R
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
-
S121A
-
site-directed mutagenesis, inactive mutant
-
Y146F
-
site-directed mutagenesis, inactive mutant
-
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
-
K151A
-
site-directed mutagenesis, inactive mutant
S123A
-
site-directed mutagenesis, inactive mutant
Y147A
-
site-directed mutagenesis, almost inactive mutant
K151A
-
site-directed mutagenesis, inactive mutant
-
S123A
-
site-directed mutagenesis, inactive mutant
-
Y147A
-
site-directed mutagenesis, almost inactive mutant
-
additional information