Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.1.3.14 - UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) and Organism(s) Escherichia coli and UniProt Accession P27828

for references in articles please use BRENDA:EC5.1.3.14
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This bacterial enzyme catalyses the reversible interconversion of UDP-GlcNAc and UDP-ManNAc. The latter is used in a variety of bacterial polysaccharide biosyntheses. cf. EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase (hydrolysing).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P27828
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
udp-n-acetylglucosamine 2-epimerase/n-acetylmannosamine kinase, udp-glcnac 2-epimerase, udp-n-acetylglucosamine 2-epimerase, udp-n-acetylglucosamine-2-epimerase/n-acetylmannosamine kinase, udp-glcnac 2-epimerase/mannac kinase, gne/mnk, cap5p, udp-n-acetylglucosamine-2-epimerase, nmsaca, udp-glcnac-2-epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-GlcNAc 2-epimerase
-
UDP-N-acetylglucosamine 2-epimerase
-
Epimerase, uridine diphosphoacetylglucosamine 2-
-
-
-
-
NeuC protein
-
-
non-hydrolyzing UDP-N-acetylglucosamine 2-epimerase
-
-
UDP-GlcNAc 2'-epimerase
-
-
-
-
UDP-GlcNAc-2-epimerase
-
-
-
-
UDP-N-acetylglucosamine 2'-epimerase
-
-
-
-
Uridine diphosphate-N-acetylglucosamine-2'-epimerase
-
-
-
-
Uridine diphospho-N-acetylglucosamine 2'-epimerase
-
-
-
-
Uridine diphosphoacetylglucosamine 2'-epimerase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine 2-epimerase
This bacterial enzyme catalyses the reversible interconversion of UDP-GlcNAc and UDP-ManNAc. The latter is used in a variety of bacterial polysaccharide biosyntheses. cf. EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase (hydrolysing).
CAS REGISTRY NUMBER
COMMENTARY hide
9037-71-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-GlcNAc
ManNAc + UDP
show the reaction diagram
biosynthetic pathway of sialic acid
-
-
?
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
r
UDP-N-acetyl-D-glucosamine
?
show the reaction diagram
-
UDP-N-acetyl-D-glucosamine 2-epimerase and UDP-N-acetyl-D-mannosamine dehydrogenase are responsible for the formation of UDP-N-acetyl-D-mannosaminuronic acid from UDP-N-acetyl-D-glucosamine
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
show the reaction diagram
additional information
?
-
-
3'-deoxy-UDP-N-acetylglucosamine is not a substrate
-
-
?
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-GlcNAc
ManNAc + UDP
show the reaction diagram
biosynthetic pathway of sialic acid
-
-
?
UDP-N-acetyl-D-glucosamine
?
show the reaction diagram
-
UDP-N-acetyl-D-glucosamine 2-epimerase and UDP-N-acetyl-D-mannosamine dehydrogenase are responsible for the formation of UDP-N-acetyl-D-mannosaminuronic acid from UDP-N-acetyl-D-glucosamine
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UDP-N-acetyl-D-glucosamine
-
allosteric activation
UDP-N-acetylglucosamine
-
the reverse reaction with UDP-N-acetylmannosamine requires the presence of UDP-N-acetylglucosamine
additional information
-
enzyme does not contain a tightly bound NAD+
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 1
UDP-N-acetyl-alpha-D-mannosamine
0.6 - 17.2
UDP-N-acetyl-D-glucosamine
0.63
UDP-N-acetylglucosamine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 7.1
UDP-N-acetyl-D-glucosamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
2 * 38000, SDS-PAGE
76000
-
gel filtraton
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 38000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, selenomethionyl enzyme, X-ray structure at 2.5 A of the enzyme with bound UDP
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C303V
exhibited almost no reduction in epimerase activity
C303X
the C303X protein does not display any enzymatic activity
D378Y
60% reduction of epimerase activity
I200F
exhibited almost no reduction in epimerase activity
D95N
-
about 18000 fold decrease in turnover number for UDP-N-acetyl-D-glucosamine, not possible to obtain accurate kinetic constants
E117Q
-
about 18000 fold decrease in turnover number for UDP-N-acetyl-D-glucosamine, not possible to obtain accurate kinetic constants
E131Q
-
about 18000 fold decrease in turnover number for UDP-N-acetyl-D-glucosamine, not possible to obtain accurate kinetic constants
H213N
-
30fold increase in Km-value and 50fold decrease in turnover-number for UDP-N-acetyl-D-glucosamine. Unlike the wild-type enzyme no inhibition is detected at UDP-concentrations up to 10 mM
K15A
-
more than 100fold increase in KM-value for UDP-N-acetyl-D-glucosamine
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes, His-tagged proteins
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Insect Cells and supercompetent InvalphaF' Escherichia coli cells (Invitrogen)
cloning of the neuC gene into an intein expression vector to facilitate purification
-
wild-type and mutant enzymes expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawamura, T.; Ichihara, N.; Ishimoto, N.; Ito, E.
Biosynthesis of uridine diphosphate N-acetyl-D-mannosaminuronic acid from uridine diphosphate N-acetyl-D-glucosamine in Escherichia coli: separation of enzymes responsible for epimerization and dehydrogenation
Biochem. Biophys. Res. Commun.
66
1506-1512
1975
Escherichia coli
Manually annotated by BRENDA team
Salo, W.L.
The incorporation of tritium from tritium-enriched water into UDP-N-acetylglucosamine and UDP-N-acetyl-mannosamine catalyzed by UDP-N-acetylglucosamine 2-epimerase from Escherichia coli
Biochim. Biophys. Acta
452
625-628
1976
Escherichia coli
Manually annotated by BRENDA team
Kawamura, T.; Kimura, M.; Yamamori, S.; Ito, E.
Enzymatic formation of uridine diphosphate N-acetyl-D-mannosamine
J. Biol. Chem.
253
3595-3601
1978
Bacillus cereus, Priestia megaterium, Bacillus subtilis, Escherichia coli, Micrococcus luteus, Staphylococcus aureus
Manually annotated by BRENDA team
Kawamura, T.; Ishimoto, N.; Ito, E.
Enzymatic synthesis of uridine diphosphate N-acetyl-D-mannosaminuronic acid
J. Biol. Chem.
254
8457-8465
1979
Escherichia coli
Manually annotated by BRENDA team
Kawamura, T.; Ishimoto, N.; Ito, E.
UDP-N-acetyl-D-glucosamine 2'-epimerase from Escherichia coli
Methods Enzymol.
83
515-519
1982
Escherichia coli
Manually annotated by BRENDA team
Sala, R.F.; Morgan, P.M.; Tanner, M.E.
Enzymic formation and release of a stable glycal intermediate: the mechanism of the reaction catalyzed by UDP-N-acetylglucosamine 2-epimerase
J. Am. Chem. Soc.
118
3033-3034
1996
Escherichia coli
-
Manually annotated by BRENDA team
Morgan, P.M.; Sala, R.F.; Tanner, M.E.
Elimination in the reactions catalyzed by UDP-N-acetylglucosamine 2-epimerase
J. Am. Chem. Soc.
119
10269-10277
1997
Escherichia coli
-
Manually annotated by BRENDA team
Campbell, R.E.; Mosimann, S.C.; Tanner, M.E.; Strynadka, N.C.
The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases
Biochemistry
39
14993-15001
2000
Escherichia coli (P27828)
Manually annotated by BRENDA team
Vann, W.F.; Daines, D.A.; Murkin, A.S.; Tanner, M.E.; Chaffin, D.O.; Rubens, C.E.; Vionnet, J.; Silver, R.P.
The NeuC protein of Escherichia coli K1 is a UDP N-acetylglucosamine 2-epimerase
J. Bacteriol.
186
706-712
2004
Escherichia coli, Escherichia coli K1
Manually annotated by BRENDA team
Samuel, J.; Tanner, M.E.
Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli
Biochim. Biophys. Acta
1700
85-91
2004
Escherichia coli
Manually annotated by BRENDA team
Penner, J.; Mantey, L.R.; Elgavish, S.; Ghaderi, D.; Cirak, S.; Berger, M.; Krause, S.; Lucka, L.; Voit, T.; Mitrani-Rosenbaum, S.; Hinderlich, S.
Influence of UDP-GlcNAc 2-epimerase/ManNAc kinase mutant proteins on hereditary inclusion body myopathy
Biochemistry
45
2968-2977
2006
Escherichia coli (P27828), Escherichia coli
Manually annotated by BRENDA team