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Information on EC 5.1.3.7 - UDP-N-acetylglucosamine 4-epimerase

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UNIPROT: Q9WYX9 not found.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
uae, udp-n-acetylglucosamine 4-epimerase, udp-n-acetylglucosamine 4'-epimerase, udp-galnac 4-epimerase, udp-glcnac epimerase, gne epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-hexose 4-epimerase
-
Epimerase, uridine diphosphoacetylglucosamine
-
-
-
-
UDP acetylglucosamine epimerase
-
-
-
-
Uridine 5'-diphospho-N-acetylglucosamine-4-epimerase
-
-
-
-
Uridine diphosphate N-acetylglucosamine-4-epimerase
-
-
-
-
Uridine diphosphoacetylglucosamine epimerase
-
-
-
-
additional information
cf. EC 5.1.3.2
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine 4-epimerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-16-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose
UDP-alpha-D-glucose
show the reaction diagram
-
-
-
r
UDP-alpha-D-glucose
UDP-alpha-D-galactose
show the reaction diagram
epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-N-acetyl-alpha-D-galactosamine
UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
additional information
?
-
enzyme TMGalE also has high activity for epimerization of UDP-Gal to UDP-Glc, EC 5.1.3.2. The catalytic efficiency (kcat/Km) for UDP-Gal is approximately 1.2 times higher than that for UDP-Glc, indicating that this enzyme might have a preference for UDP-Gal over UDP-Glc. The catalytic efficiencies of TMGalE for UDP-GalNAc and UDP-GlcNAc are approximately 25fold and 10fold higher than those for UDP-Gal and UDP-Glc, respectively
-
-
?
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-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
enzyme-bound, exogenous NAD+ does not appear to be a strong activator of enzyme activity, there is no significant difference in enzyme activity regardless of the presence and absence of NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme is not specifically dependent on divalent metal ions for its catalytic activity, negligible effects by Co2+, Mn2+, Mg2+, Zn2+, Ca2+, Cu2+, Fe2+, or Ni2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.53
UDP-alpha-D-galactose
pH 7.0, 80°C
12.9
UDP-alpha-D-glucose
pH 7.0, 80°C
1.06 - 2.4
UDP-N-acetyl-alpha-D-galactosamine
1.06 - 2.4
UDP-N-acetyl-alpha-D-glucosamine
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7757
UDP-alpha-D-galactose
pH 7.0, 80°C
14677
UDP-alpha-D-glucose
pH 7.0, 80°C
27671 - 38295
UDP-N-acetyl-alpha-D-galactosamine
27671 - 38295
UDP-N-acetyl-alpha-D-glucosamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1406
UDP-alpha-D-galactose
pH 7.0, 80°C
1134
UDP-alpha-D-glucose
pH 7.0, 80°C
11465 - 36120
UDP-N-acetyl-alpha-D-galactosamine
11465 - 36120
UDP-N-acetyl-alpha-D-glucosamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48.7
purified recombinant enzyme, pH 7.0.80°C, substrate UDP-N-acetyl-glucosamine
93.7
purified recombinant enzyme, pH 7.0.80°C, substrate UDP-N-acetyl-galactosamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
6 - 8
over 95% of maximal activity within this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 100
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.72
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in D-galactose metabolism
physiological function
UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for D-galactose metabolism
additional information
dinucleotide-binding pocket in the active site, and conformational changes in the active site of TMGalE, ligand binding sites of TMGalE in complex with NAD+and UDP-Glc
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9WYX9_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
309
0
34900
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
enzyme structure analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of the enzyme (TMGalE) and the enzyme bound to UDP-glucose is determined at resolutions of 1.9 A and 2.0 A, respectively
purified recombinant unbound enzyme TMGalE, and TMGalE bound to UDP-Glc, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in in Escherichia coli
gene galE, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression in and functional complementation of enzyme-deficient Escherichia coli strain BW25113 DELTAgalE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shin, S.; Choi, J.; Di Luccio, E.; Lee, Y.; Lee, S.; Lee, S.; Lee, S.; Lee, D.
The structural basis of substrate promiscuity in UDP-hexose 4-epimerase from the hyperthermophilic Eubacterium Thermotoga maritima
Arch. Biochem. Biophys.
585
39-51
2015
Thermotoga maritima (Q9WYX9), Thermotoga maritima DSM 3109 (Q9WYX9), Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 (Q9WYX9)
Manually annotated by BRENDA team