5.1.3.7: UDP-N-acetylglucosamine 4-epimerase
This is an abbreviated version!
For detailed information about UDP-N-acetylglucosamine 4-epimerase, go to the full flat file.
Word Map on EC 5.1.3.7
-
5.1.3.7
-
emirates
-
artery
-
albumin
-
urinary
-
uterine
-
embolization
-
women
-
microalbuminuria
-
fibroid
-
ultrasound
-
hypertension
-
ultrasound-assisted
-
symptomatic
-
mellitus
-
cardiovascular
-
nephropathy
-
glomerular
-
pregnancy
-
hysterectomy
-
creatinine
-
albuminuria
-
systolic
-
bleeding
-
gulf
-
diastolic
-
ultrasonic
-
dubai
-
ambulatory
-
arabia
-
cesarean
-
normoalbuminuric
-
myomectomy
-
antihypertensive
-
microwave-assisted
-
menorrhagia
-
curettage
-
qatar
-
myoma
-
adenomyosis
-
box-behnken
-
hypertensives
-
kuwait
-
leiomyomata
-
postprocedural
-
citizens
-
soxhlet
-
satisfaction
-
radiologist
-
synthesis
-
medicine
-
transvaginal
-
preprocedural
- 5.1.3.7
-
emirates
- artery
- albumin
- urinary
- uterine
-
embolization
- women
-
microalbuminuria
- fibroid
-
ultrasound
- hypertension
-
ultrasound-assisted
-
symptomatic
- mellitus
- cardiovascular
- nephropathy
-
glomerular
- pregnancy
-
hysterectomy
- creatinine
- albuminuria
-
systolic
- bleeding
-
gulf
-
diastolic
-
ultrasonic
-
dubai
-
ambulatory
- arabia
-
cesarean
-
normoalbuminuric
-
myomectomy
-
antihypertensive
-
microwave-assisted
- menorrhagia
-
curettage
-
qatar
- myoma
- adenomyosis
-
box-behnken
-
hypertensives
-
kuwait
-
leiomyomata
-
postprocedural
-
citizens
-
soxhlet
-
satisfaction
-
radiologist
- synthesis
- medicine
-
transvaginal
-
preprocedural
Reaction
Synonyms
Epimerase, uridine diphosphoacetylglucosamine, Galactowaldenase, GalE, galE-2, GalESp2, GNE, Gne epimerase, group 3 epimerase, KfoA, More, TM0509, TMGalE, UAE, UDP acetylglucosamine epimerase, UDP-galactose 4-epimerase, UDP-galactose-4-epimerase, UDP-GalNAc 4-epimerase, UDP-Glc(NAc) 4-epimerase, UDP-GlcNAc 4-epimerase, UDP-GlcNAc epimerase, UDP-GlcNAc/Glc 4-epimerase, UDP-hexose 4-epimerase, UDP-N-acetylglucosamine 4'-epimerase, UDP-N-acetylglucosamine 4-epimerase, UDP-N-acetylglucosamine-4'-epimerase, UDP-sugar 4-epimerase, UDPGlcNAc 4-epimerase, Uridine 5'-diphospho-N-acetylglucosamine-4-epimerase, Uridine diphosphate N-acetylglucosamine-4-epimerase, Uridine diphosphoacetylglucosamine epimerase, WbgU, WbPP
ECTree
5.1.3.7 UDP-N-acetylglucosamine 4-epimeraseAdvanced search results
results (
results (Engineering
Engineering on EC 5.1.3.7 - UDP-N-acetylglucosamine 4-epimerase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H305A
-
site-directed mutagenesis, structure determination and analysis, the mutant shows reduced activity with UDP-N-acetylglucosamine
S144T/H305A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine
S144T/R304G/H305A
-
site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine
S144T/R304G/H305A/S306Y
-
site-directed mutagenesis, the mutant shows no activity with either UDP-GlcNAc or UDP-Glc
S301Y
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
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
A209H
A209N
G102K
G102K/Q201E
site-directed mutagenesis, as a result of the introduction of both mutations at the same time, a salt bridge is formed, which results in a rescue of the activity for acetylated substrates, probably due to restoration of the slight distortion that is observed in both single mutants
Q201E
Q201E/G102K
-
mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine, no epimerization activity with UDP-D-glucose and very limited activity with UDP-D-galactose
S143A
-
mutant enzyme shows epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine similar to wild-type enzyme and no epimerization activity with UDP-D-glucose and UDP-D-galactose
S144K
-
mutant enzyme shows no epimerization activity with UDP-N-acetyl-D-glucosamine/UDP-N-acetyl-D-galactosamine and UDP-D-glucose/UDP-D-galactose
S306Y
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
S301Y
site-directed mutagenesis, the mutation in KfoA results in loss of UDP-GlcNAc/UDP-GalNAc conversion activity
S301Y
Escherichia coli ATCC 23502 / K4
-
site-directed mutagenesis, the mutation in KfoA results in loss of UDP-GlcNAc/UDP-GalNAc conversion activity
-
A209H
-
mutant enzyme shows very limited epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and slightly reduced epimerization activity with UDP-D-glucose and UDP-D-galactose
A209H
-
unlike the wild-type enzyme the mutant enzyme is more efficient in catalyzing the reaction with the non-acetylated hexoses UDP-glucose and UDP-galactose than in catalyzing epimerization of UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine
A209H
site-directed mutagenesis, the mutation results in limited ability to epimerize acetylated residues
A209N
-
mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and very limited epimerization activity with UDP-D-glucose and UDP-D-galactose
A209N
site-directed mutagenesis, the mutation enhances the specificity for acetylated substrates accompanied by a lower catalytic efficiency
G102K
-
mutant enzyme shows slightly reduced epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine and no epimerization activity with UDP-D-glucose and UDP-D-galactose
G102K
site-directed mutagenesis, the mutation slightly reduces activity on acetylated substrates and almost abolishes activity on non-acetylated substrates
Q201E
-
mutant enzyme shows slightly epimerization activity with UDP-N-acetyl-D-glucosamine and UDP-N-acetyl-D-galactosamine similar to wild-type activity and very limited epimerization activity with UDP-D-Glc and UDP-D-Gal
Q201E
site-directed mutagenesis, the mutation slightly reduces activity on acetylated substrates and almost abolishes activity on non-acetylated substrates
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. The S306Y mutation in WbpP totally abolishes the activity of the enzyme
additional information
silencing gene GALE with specific siRNAs in human chondrocytes
additional information
a gne-deficient mutant completely lacks UDPGalNAc 4-epimerase activity and has UDP-Gal 4-epimerase activity in after growth on D-glucose or D-galactose that is not significantly different from that of the wild-type strain. Mutation increases the surface hydrophobicity, produces deep alterations in the outer membrane architecture, and results in noticeable increases in the sensitivity to microcidal peptides, to eel and human sera, and to phagocytosis/opsonophagocytosis. Significant attenuation of virulence for eels and mice is observed with the mutant
additional information
-
a gne-deficient mutant completely lacks UDPGalNAc 4-epimerase activity and has UDP-Gal 4-epimerase activity in after growth on D-glucose or D-galactose that is not significantly different from that of the wild-type strain. Mutation increases the surface hydrophobicity, produces deep alterations in the outer membrane architecture, and results in noticeable increases in the sensitivity to microcidal peptides, to eel and human sera, and to phagocytosis/opsonophagocytosis. Significant attenuation of virulence for eels and mice is observed with the mutant
