Any feedback?
Literature summary for 5.1.3.2 extracted from
- Role of galE on biofilm formation by Thermus spp. (2009), Biochem. Biophys. Res. Commun., 390, 313-318.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged enzyme | Thermus aquaticus |
| expression of the enzyme obtained from HB8 strain in Escherichia coli as His-tagged protein | Thermus thermophilus |
| recombinant enzyme overexpression in Thermus thermophilus strain HB27 to an increased capacity of biofilm production, expression of His-tagged enzyme | Thermus thermophilus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.258 | - |
UDP-galactose | pH 8.9, 50°C, recombinant GalE | Thermus thermophilus |  |
| 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
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| MgCl2 | is included in assay medium | Thermus thermophilus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 35000 | - |
determined by SDS-PAGE and MALDI-TOF mass spectrometry | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | ? | - |
? | |
| 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 | - |
? | |
| 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 | |
| UDP-galactose | Thermus thermophilus | - |
UDP-glucose | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus aquaticus | - |
strains YT-1 and NTU103, gene galE | - |
| Thermus thermophilus | - |
- |
- |
| Thermus thermophilus | - |
strains HB8 and HB27, gene galE | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| by using nickel-NTA affinity chromatography | Thermus thermophilus |
| recombinant His-tagged enzyme by nickel affinity chromatography | Thermus aquaticus |
| recombinant His-tagged enzyme by nickel affinity chromatography | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | ? | - |
? | |
| UDP-alpha-D-glucose | - |
Thermus aquaticus | UDP-alpha-D-galactose | - |
r | |
| UDP-alpha-D-glucose | - |
Thermus thermophilus | UDP-alpha-D-galactose | - |
r | |
| 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 | - |
? | |
| 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 | |
| UDP-galactose | - |
Thermus thermophilus | UDP-glucose | - |
r | |
| UDP-N-acetylgalactosamine | - |
Thermus thermophilus | UDP-N-acetylglucosamine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Thermus aquaticus |
| homodimer | - |
Thermus thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GalE | - |
Thermus aquaticus |
| GalE | - |
Thermus thermophilus |
| UDP-galactose-4'-epimerase | - |
Thermus aquaticus |
| UDP-galactose-4'-epimerase | - |
Thermus thermophilus |
| uridine diphosphate-galactose-4'-epimerase | - |
Thermus aquaticus |
| uridine diphosphate-galactose-4'-epimerase | - |
Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Thermus thermophilus |
| 50 | - |
recombinant enzyme | Thermus thermophilus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
purified recombinant enzyme, 30 min, loss of 78% activity | Thermus thermophilus |
| 80 | - |
treatment at 80°C for 30 min reduces the enzyme activity by 78% | Thermus thermophilus |
| 90 | - |
enzyme is stable at 90°C, after incubating at this temperature for 10 min, 90% of the enzymatic activity remains | Thermus thermophilus |
| 90 | - |
purified recombinant enzyme, 10 min, loss of 10% activity | Thermus thermophilus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 55.32 | - |
UDP-galactose | pH 8.9, 50°C, recombinant GalE | Thermus thermophilus | |
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.9 | - |
assay at | Thermus aquaticus |
| 9 | - |
- |
Thermus thermophilus |
| 9 | - |
recombinant enzyme | Thermus thermophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Thermus thermophilus | |
| NAD+ | bound to the enzyme via GxxGxxG motif | Thermus aquaticus | |
| NAD+ | bound to the enzyme via GxxGxxG motif | Thermus thermophilus | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Thermus thermophilus | overexpression in Thermus thermophilus HB27 leads to an increased capacity of biofilm production | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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 | |
| 214.4 | - |
UDP-galactose | pH 8.9, 50°C, recombinant GalE | Thermus thermophilus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
