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Literature summary extracted from

  • 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 (2015), Arch. Biochem. Biophys., 585, 39-51 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.3.2 expression in in Escherichia coli Thermotoga maritima
5.1.3.2 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 Thermotoga maritima
5.1.3.7 expression in in Escherichia coli Thermotoga maritima
5.1.3.7 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 Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.3.2 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 Thermotoga maritima
5.1.3.2 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 Thermotoga maritima
5.1.3.7 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 Thermotoga maritima
5.1.3.7 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 Thermotoga maritima

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.2 additional information
-
additional information Michaelis-Menten kinetics Thermotoga maritima
5.1.3.2 1.06
-
UDP-N-acetyl-alpha-D-galactosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.2 2.4
-
UDP-N-acetyl-alpha-D-glucosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.2 5.53
-
UDP-alpha-D-galactose pH 7.0, 80°C Thermotoga maritima
5.1.3.2 5.53
-
UDP-alpha-D-glucose recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.2 12.9
-
UDP-alpha-D-glucose pH 7.0, 80°C Thermotoga maritima
5.1.3.2 12.9
-
UDP-alpha-D-galactose recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.7 additional information
-
additional information Michaelis-Menten kinetics Thermotoga maritima
5.1.3.7 1.06
-
UDP-N-acetyl-alpha-D-galactosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.7 1.06
-
UDP-N-acetyl-alpha-D-glucosamine recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.7 2.4
-
UDP-N-acetyl-alpha-D-glucosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.7 2.4
-
UDP-N-acetyl-alpha-D-galactosamine recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.7 5.53
-
UDP-alpha-D-galactose pH 7.0, 80°C Thermotoga maritima
5.1.3.7 12.9
-
UDP-alpha-D-glucose pH 7.0, 80°C Thermotoga maritima

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.3.2 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+ Thermotoga maritima
5.1.3.7 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+ Thermotoga maritima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.3.2 70000
-
gel filtration Thermotoga maritima
5.1.3.2 70000
-
recombinant His6-tagged enzyme, gel filtration Thermotoga maritima
5.1.3.7 70000
-
gel filtration Thermotoga maritima
5.1.3.7 70000
-
recombinant His6-tagged enzyme, gel filtration Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.3.2 UDP-alpha-D-glucose Thermotoga maritima
-
UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose Thermotoga maritima DSM 3109
-
UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099
-
UDP-alpha-D-galactose
-
r
5.1.3.7 UDP-N-acetyl-alpha-D-glucosamine Thermotoga maritima
-
UDP-N-acetyl-alpha-D-galactosamine
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.2 Thermotoga maritima Q9WYX9
-
-
5.1.3.2 Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 Q9WYX9
-
-
5.1.3.2 Thermotoga maritima DSM 3109 Q9WYX9
-
-
5.1.3.7 Thermotoga maritima Q9WYX9
-
-
5.1.3.7 Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 Q9WYX9
-
-
5.1.3.7 Thermotoga maritima DSM 3109 Q9WYX9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.3.2
-
Thermotoga maritima
5.1.3.2 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Thermotoga maritima
5.1.3.7
-
Thermotoga maritima
5.1.3.7 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Thermotoga maritima

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.3.2 69.7
-
purified recombinant enzyme, pH 7.0, 80°C, substrate UDP-glucose Thermotoga maritima
5.1.3.2 192.4
-
purified recombinant enzyme, pH 7.0, 80°C, substrate UDP-galactose Thermotoga maritima
5.1.3.7 48.7
-
purified recombinant enzyme, pH 7.0.80°C, substrate UDP-N-acetyl-glucosamine Thermotoga maritima
5.1.3.7 93.7
-
purified recombinant enzyme, pH 7.0.80°C, substrate UDP-N-acetyl-galactosamine Thermotoga maritima

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.2 additional information enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. 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 Thermotoga maritima ?
-
?
5.1.3.2 additional information enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. 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 Thermotoga maritima DSM 3109 ?
-
?
5.1.3.2 additional information enzyme TMGalE also has an unusually high activity for epimerization of UDP-GalNAc to UDP-GlcNAc, EC 5.1.3.7. 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 Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 ?
-
?
5.1.3.2 UDP-alpha-D-galactose
-
Thermotoga maritima UDP-alpha-D-glucose
-
r
5.1.3.2 UDP-alpha-D-galactose enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium Thermotoga maritima UDP-alpha-D-glucose
-
r
5.1.3.2 UDP-alpha-D-galactose
-
Thermotoga maritima DSM 3109 UDP-alpha-D-glucose
-
r
5.1.3.2 UDP-alpha-D-galactose
-
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 UDP-alpha-D-glucose
-
r
5.1.3.2 UDP-alpha-D-glucose
-
Thermotoga maritima UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium Thermotoga maritima UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose Thermotoga maritima UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose
-
Thermotoga maritima DSM 3109 UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium Thermotoga maritima DSM 3109 UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose Thermotoga maritima DSM 3109 UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose
-
Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose enzyme TMGalE has higher activity toward UDP-Gal with the 1:3 conversion ratio of UDP-Gal to UDP-Glc at equilibrium Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-alpha-D-glucose epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose Thermotoga maritima ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 UDP-alpha-D-galactose
-
r
5.1.3.2 UDP-N-acetyl-alpha-D-galactosamine epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose Thermotoga maritima UDP-N-acetyl-alpha-D-glucosamine
-
r
5.1.3.2 UDP-N-acetyl-alpha-D-glucosamine epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose Thermotoga maritima UDP-N-acetyl-alpha-D-galactosamine
-
r
5.1.3.7 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 Thermotoga maritima ?
-
?
5.1.3.7 UDP-alpha-D-galactose
-
Thermotoga maritima UDP-alpha-D-glucose
-
r
5.1.3.7 UDP-alpha-D-glucose epimerization at 36.2% compared to the activity with UDP-alpha-D-galactose Thermotoga maritima UDP-alpha-D-galactose
-
r
5.1.3.7 UDP-N-acetyl-alpha-D-galactosamine epimerization at 48.5% compared to the activity with UDP-alpha-D-galactose Thermotoga maritima UDP-N-acetyl-alpha-D-glucosamine
-
r
5.1.3.7 UDP-N-acetyl-alpha-D-glucosamine
-
Thermotoga maritima UDP-N-acetyl-alpha-D-galactosamine
-
r
5.1.3.7 UDP-N-acetyl-alpha-D-glucosamine epimerization at 25.3% compared to the activity with UDP-alpha-D-galactose Thermotoga maritima UDP-N-acetyl-alpha-D-galactosamine
-
r

Subunits

EC Number Subunits Comment Organism
5.1.3.2 homodimer 2 * 35000, SDS-PAGE Thermotoga maritima
5.1.3.2 homodimer 2 * 34899, calculated from sequence Thermotoga maritima
5.1.3.2 homodimer 2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation Thermotoga maritima
5.1.3.2 More enzyme structure analysis, overview Thermotoga maritima
5.1.3.7 homodimer 2 * 35000, SDS-PAGE Thermotoga maritima
5.1.3.7 homodimer 2 * 34899, calculated from sequence Thermotoga maritima
5.1.3.7 homodimer 2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE, 2 * 34899, sequence calculation Thermotoga maritima
5.1.3.7 More enzyme structure analysis, overview Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
5.1.3.2 GalE
-
Thermotoga maritima
5.1.3.2 More cf. EC 5.1.3.7 Thermotoga maritima
5.1.3.2 TM0509
-
Thermotoga maritima
5.1.3.2 TMGalE
-
Thermotoga maritima
5.1.3.2 UDP-galactose 4-epimerase
-
Thermotoga maritima
5.1.3.2 UDP-hexose 4-epimerase
-
Thermotoga maritima
5.1.3.7 GalE
-
Thermotoga maritima
5.1.3.7 More cf. EC 5.1.3.2 Thermotoga maritima
5.1.3.7 TM0509
-
Thermotoga maritima
5.1.3.7 TMGalE
-
Thermotoga maritima
5.1.3.7 UDP-hexose 4-epimerase
-
Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.3.2 80
-
-
Thermotoga maritima
5.1.3.7 80
-
-
Thermotoga maritima

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.1.3.2 30 100 over 50% of maximal activity within this range Thermotoga maritima
5.1.3.2 30 100 30°C: 53% of the maximal activity, 100°C: 90% of maximal activity Thermotoga maritima
5.1.3.7 30 100 over 50% of maximal activity within this range Thermotoga maritima
5.1.3.7 30 100 30°C: 53% of the maximal activity, 100°C: 90% of maximal activity Thermotoga maritima

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.3.2 70
-
3 h, no significant decrease in activity Thermotoga maritima
5.1.3.2 70
-
purified recombinant His6-tagged enzyme, no significant decrease in enzyme activity after 3 h Thermotoga maritima
5.1.3.2 80
-
3 h, the enzyme retains more than 85% of its original activity Thermotoga maritima
5.1.3.2 80
-
purified recombinant His6-tagged enzyme, retains more than 85% of its original activity under standard assay conditions after 3 h Thermotoga maritima
5.1.3.2 90
-
40 min, almost 50% of its original activity Thermotoga maritima
5.1.3.2 90
-
purified recombinant His6-tagged enzyme, retains 50% of its original activity under standard assay conditions after 40 min Thermotoga maritima
5.1.3.7 70
-
3 h, no significant decrease in activity Thermotoga maritima
5.1.3.7 70
-
purified recombinant His6-tagged enzyme, no significant decrease in enzyme activity after 3 h Thermotoga maritima
5.1.3.7 80
-
3 h, the enzyme retains more than 85% of its original activity Thermotoga maritima
5.1.3.7 80
-
purified recombinant His6-tagged enzyme, retains more than 85% of its original activity under standard assay conditions after 3 h Thermotoga maritima
5.1.3.7 90
-
40 min, almost 50% of its original activity Thermotoga maritima
5.1.3.7 90
-
purified recombinant His6-tagged enzyme, retains 50% of its original activity under standard assay conditions after 40 min Thermotoga maritima

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.3.2 7757
-
UDP-alpha-D-galactose pH 7.0, 80°C Thermotoga maritima
5.1.3.2 7757
-
UDP-alpha-D-glucose recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.2 14677
-
UDP-alpha-D-glucose pH 7.0, 80°C Thermotoga maritima
5.1.3.2 14677
-
UDP-alpha-D-galactose recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.2 27671
-
UDP-N-acetyl-alpha-D-glucosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.2 38295
-
UDP-N-acetyl-alpha-D-galactosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.7 7757
-
UDP-alpha-D-galactose pH 7.0, 80°C Thermotoga maritima
5.1.3.7 14677
-
UDP-alpha-D-glucose pH 7.0, 80°C Thermotoga maritima
5.1.3.7 27671
-
UDP-N-acetyl-alpha-D-glucosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.7 27671
-
UDP-N-acetyl-alpha-D-galactosamine recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.7 38295
-
UDP-N-acetyl-alpha-D-galactosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.7 38295
-
UDP-N-acetyl-alpha-D-glucosamine recombinant enzyme, pH 7.0, 80°C Thermotoga maritima

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.3.2 7
-
-
Thermotoga maritima
5.1.3.7 7
-
-
Thermotoga maritima

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.3.2 5 10 over 50% of maximal activity within this range Thermotoga maritima
5.1.3.2 5 10 pH 5.0: about 50% of maximal activity, pH 10: about 55% of maximal activity Thermotoga maritima
5.1.3.2 6 8 over 95% of maximal activity within this range Thermotoga maritima
5.1.3.7 5 10 over 50% of maximal activity within this range Thermotoga maritima
5.1.3.7 5 10 pH 5.0: about 50% of maximal activity, pH 10: about 55% of maximal activity Thermotoga maritima
5.1.3.7 6 8 over 95% of maximal activity within this range Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.3.2 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+ Thermotoga maritima
5.1.3.7 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+ Thermotoga maritima

pI Value

EC Number Organism Comment pI Value Maximum pI Value
5.1.3.2 Thermotoga maritima sequence calculation
-
5.72
5.1.3.7 Thermotoga maritima sequence calculation
-
5.72

General Information

EC Number General Information Comment Organism
5.1.3.2 metabolism the enzyme is involved in D-galactose metabolism Thermotoga maritima
5.1.3.2 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 Thermotoga maritima
5.1.3.2 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 Thermotoga maritima
5.1.3.7 metabolism the enzyme is involved in D-galactose metabolism Thermotoga maritima
5.1.3.7 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 Thermotoga maritima
5.1.3.7 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 Thermotoga maritima

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.1.3.2 1134
-
UDP-alpha-D-glucose pH 7.0, 80°C Thermotoga maritima
5.1.3.2 1134
-
UDP-alpha-D-galactose recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.2 1406
-
UDP-alpha-D-galactose pH 7.0, 80°C Thermotoga maritima
5.1.3.2 1406
-
UDP-alpha-D-glucose recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.2 11465
-
UDP-N-acetyl-alpha-D-glucosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.2 36120
-
UDP-N-acetyl-alpha-D-galactosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.7 1134
-
UDP-alpha-D-glucose pH 7.0, 80°C Thermotoga maritima
5.1.3.7 1406
-
UDP-alpha-D-galactose pH 7.0, 80°C Thermotoga maritima
5.1.3.7 11465
-
UDP-N-acetyl-alpha-D-glucosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.7 11465
-
UDP-N-acetyl-alpha-D-galactosamine recombinant enzyme, pH 7.0, 80°C Thermotoga maritima
5.1.3.7 36120
-
UDP-N-acetyl-alpha-D-galactosamine pH 7.0, 80°C Thermotoga maritima
5.1.3.7 36120
-
UDP-N-acetyl-alpha-D-glucosamine recombinant enzyme, pH 7.0, 80°C Thermotoga maritima