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Literature summary extracted from

  • Niou, Y.K.; Wu, W.L.; Lin, L.C.; Yu, M.S.; Shu, H.Y.; Yang, H.H.; Lin, G.H.
    Role of galE on biofilm formation by Thermus spp. (2009), Biochem. Biophys. Res. Commun., 390, 313-318.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.3.2 expression of His-tagged enzyme Thermus aquaticus
5.1.3.2 expression of the enzyme obtained from HB8 strain in Escherichia coli as His-tagged protein Thermus thermophilus
5.1.3.2 recombinant enzyme overexpression in Thermus thermophilus strain HB27 to an increased capacity of biofilm production, expression of His-tagged enzyme Thermus thermophilus
5.1.3.7 expression of the enzyme obtained from HB8 strain in Escherichia coli as His-tagged protein Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.2 0.258
-
 UDP-galactose pH 8.9, 50°C, recombinant GalE Thermus thermophilus
5.1.3.2 0.258
-
 UDP-galactose recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.3.2 MgCl2 is included in assay medium Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.3.2 35000
-
 determined by SDS-PAGE and MALDI-TOF mass spectrometry Thermus thermophilus
5.1.3.7 35000
-
 determined by SDS-PAGE and MALDI-TOF mass spectrometry Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.3.2 additional information Thermus thermophilus both enzymatic activities, as uridine diphosphate-galactose-4'-epimerase and UDP-N-acetylglucosamine-4'-epimerase, reveal that enzyme from Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-glucose to UDP-galactose and between their N-acetylated forms ?
-
 ?
5.1.3.2 UDP-alpha-D-glucose Thermus aquaticus the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis UDP-alpha-D-galactose
-
 ?
5.1.3.2 UDP-alpha-D-glucose Thermus thermophilus the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis UDP-alpha-D-galactose
-
 r
5.1.3.2 UDP-galactose Thermus thermophilus
-
 UDP-glucose
-
 r
5.1.3.7 additional information Thermus thermophilus Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-D-glucose to UDP-D-galactose and between their N-acetylated forms ?
-
 ?
5.1.3.7 UDP-N-acetylgalactosamine Thermus thermophilus GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner UDP-N-acetylglucosamine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.2 Thermus aquaticus
-
 strains YT-1 and NTU103, gene galE
-
5.1.3.2 Thermus thermophilus
-
-
-
5.1.3.2 Thermus thermophilus
-
 strains HB8 and HB27, gene galE
-
5.1.3.7 Thermus thermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.3.2 by using nickel-NTA affinity chromatography Thermus thermophilus
5.1.3.2 recombinant His-tagged enzyme by nickel affinity chromatography Thermus aquaticus
5.1.3.2 recombinant His-tagged enzyme by nickel affinity chromatography Thermus thermophilus
5.1.3.7 by using nickel-NTA affinity chromatography Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.2 additional information both enzymatic activities, as uridine diphosphate-galactose-4'-epimerase and UDP-N-acetylglucosamine-4'-epimerase, reveal that enzyme from Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-glucose to UDP-galactose and between their N-acetylated forms Thermus thermophilus ?
-
 ?
5.1.3.2 UDP-alpha-D-glucose
-
 Thermus aquaticus UDP-alpha-D-galactose
-
 r
5.1.3.2 UDP-alpha-D-glucose
-
 Thermus thermophilus UDP-alpha-D-galactose
-
 r
5.1.3.2 UDP-alpha-D-glucose the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis Thermus aquaticus UDP-alpha-D-galactose
-
 ?
5.1.3.2 UDP-alpha-D-glucose the enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis Thermus thermophilus UDP-alpha-D-galactose
-
 r
5.1.3.2 UDP-galactose
-
 Thermus thermophilus UDP-glucose
-
 r
5.1.3.2 UDP-N-acetylgalactosamine
-
 Thermus thermophilus UDP-N-acetylglucosamine
-
 ?
5.1.3.7 additional information Thermus thermophilus HB8 show dual functions for catalyzing conversion of UDP-D-glucose to UDP-D-galactose and between their N-acetylated forms Thermus thermophilus ?
-
 ?
5.1.3.7 UDP-N-acetylgalactosamine GalE epimerizes UDP-N-acetylgalactosamine in a dose-dependent manner Thermus thermophilus UDP-N-acetylglucosamine
-
 r

Subunits

EC Number Subunits Comment Organism
5.1.3.2 homodimer
-
 Thermus aquaticus
5.1.3.2 homodimer
-
 Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
5.1.3.2 GalE
-
 Thermus aquaticus
5.1.3.2 GalE
-
 Thermus thermophilus
5.1.3.2 UDP-galactose-4'-epimerase
-
 Thermus aquaticus
5.1.3.2 UDP-galactose-4'-epimerase
-
 Thermus thermophilus
5.1.3.2 uridine diphosphate-galactose-4'-epimerase
-
 Thermus aquaticus
5.1.3.2 uridine diphosphate-galactose-4'-epimerase
-
 Thermus thermophilus
5.1.3.7 GalE
-
 Thermus thermophilus
5.1.3.7 UDP-N-acetylglucosamine-4'-epimerase
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.3.2 50
-
-
 Thermus thermophilus
5.1.3.2 50
-
 recombinant enzyme Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.3.2 80
-
 purified recombinant enzyme, 30 min, loss of 78% activity Thermus thermophilus
5.1.3.2 80
-
 treatment at 80°C for 30 min reduces the enzyme activity by 78% Thermus thermophilus
5.1.3.2 90
-
 enzyme is stable at 90°C, after incubating at this temperature for 10 min, 90% of the enzymatic activity remains Thermus thermophilus
5.1.3.2 90
-
 purified recombinant enzyme, 10 min, loss of 10% activity Thermus thermophilus
5.1.3.7 80
-
 treatment at 80 °C for 30 min reduces the enzyme activity by 78% Thermus thermophilus
5.1.3.7 90
-
 enzyme is stable at 90°C; after incubating at this temperature for 10 min, 90% of the enzymatic activity remains Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.3.2 55.32
-
 UDP-galactose pH 8.9, 50°C, recombinant GalE Thermus thermophilus
5.1.3.2 199.1
-
 UDP-galactose recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.3.2 8.9
-
 assay at Thermus aquaticus
5.1.3.2 9
-
-
 Thermus thermophilus
5.1.3.2 9
-
 recombinant enzyme Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.3.2 NAD+
-
 Thermus thermophilus
5.1.3.2 NAD+ bound to the enzyme via GxxGxxG motif Thermus aquaticus
5.1.3.2 NAD+ bound to the enzyme via GxxGxxG motif Thermus thermophilus

Expression

EC Number Organism Comment Expression
5.1.3.2 Thermus thermophilus overexpression in Thermus thermophilus HB27 leads to an increased capacity of biofilm production up
5.1.3.7 Thermus thermophilus overexpression in Thermus thermophilus HB27 leads to an increased capacity of biofilm production up

General Information

EC Number General Information Comment Organism
5.1.3.2 physiological function enzyme catalyzes the conversion of UDP-galactose to UDP-glucose, an important biochemical step in exopolysaccharide synthesis, gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis Thermus thermophilus
5.1.3.2 physiological function galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis Thermus aquaticus
5.1.3.2 physiological function galE gene is important to biofilm formation because of its involvement in epimerizing UDP-galactose and UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis Thermus thermophilus
5.1.3.7 physiological function gene is important to biofilm formation because of its involvement in epimerizing UDP-N-acetylgalactosamine for exopolysaccharide biosynthesis Thermus thermophilus

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 0.78
-
 UDP-galactose recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase Thermus thermophilus
5.1.3.2 214.4
-
 UDP-galactose pH 8.9, 50°C, recombinant GalE Thermus thermophilus