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Literature summary for 5.1.3.2 extracted from
- Chemical and stereochemical actions of UDP-galactose 4-epimerase (2013), Acc. Chem. Res., 46, 1417-1426.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K153M | site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme | Escherichia coli |
| additional information | second-order rate constants for reductive inactivation of wild-type and mutant epimerases, overview | Escherichia coli |
| S124A | site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme | Escherichia coli |
| S124T | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Escherichia coli |
| Y149F | site-directed mutagenesis, the mutant shows reduced highly activity compared to the wild-type enzyme | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2 | 6 | UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant Y149F | Escherichia coli |  |
| 83 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant K153M | Escherichia coli | |
| 110 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant S124A | Escherichia coli | |
| 230 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme | Escherichia coli | |
| 260 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant S124T | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-alpha-D-glucose | Escherichia coli | - |
UDP-alpha-D-galactose | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
gene galE | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| UDP-alpha-D-glucose = UDP-alpha-D-galactose | structurereactivity studies and reaction mode, acid-base catalysis of hydride transfer, overview | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-alpha-D-glucose | - |
Escherichia coli | UDP-alpha-D-galactose | - |
? | |
| UDP-alpha-D-glucose | with NAD+ as cofactor, UDP-4-ketopyranose and NADH are reaction intermediates. Weak binding of the 4-ketopyranosyl moiety and strong binding of the UDP-moiety within a substrate domain allow either face of the 4-ketopyranosyl moiety to accept hydride from NADH, pH-dependent charge transfer complex between Tyr149 and NAD+ | Escherichia coli | UDP-alpha-D-galactose | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | fully active enzyme | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GalE | - |
Escherichia coli |
| UDP-galactose 4-epimerase | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.073 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant Y149F | Escherichia coli | |
| 0.61 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant S124A | Escherichia coli | |
| 0.67 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant K153M | Escherichia coli | |
| 250 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant S124T | Escherichia coli | |
| 760 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme | Escherichia coli | |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9 | pH-dependencies of wild-type and mutant enzymes, overview | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | the fully active GalE is dimeric and contains one tightly bound NAD+ per subunit, NAD+ undergoes reversible reduction to NADH in the chemical mechanism, practically irreversible binding of NAD+ within a Rossmann-type fold, nonstereospecific hydride transfer, uridine nucleotide-induced activation of NAD, Tyr149 as a base catalyst, and [GalE-NADH]-oxidation in one-electron steps by one-electron acceptors. pH-Dependent charge transfer complex between Tyr149 and NAD+. Binding structure, overview | Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | ligand-bound enzyme structures, active site structure including Lys153, Tyr149, and Ser124, overview | Escherichia coli |
| physiological function | UDP-Gal provides all galactosyl units in biologically synthesized carbohydrates. All healthy cells produce UDP-Gal from uridine 5'-diphospho-alpha-D-glucose UDP-Glc, by the action of UDP-galactose 4-epimerase | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.9 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant Y149F | Escherichia coli | |
| 5.5 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant S124A | Escherichia coli | |
| 8.1 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant mutant K153M | Escherichia coli | |
| 970 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant S124T | Escherichia coli | |
| 3400 | - |
UDP-alpha-D-glucose | pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme | Escherichia coli | |
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