Any feedback?
Literature summary for 5.1.3.7 extracted from
- Characterization and mutational analysis of the UDP-Glc(NAc) 4-epimerase from Marinithermus hydrothermalis (2013), Appl. Microbiol. Biotechnol., 97, 7733-7740.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene galE, expression of N-termminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Marinithermus hydrothermalis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G118A/G119A | site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates | Marinithermus hydrothermalis |
| G188S/G119S | site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates | Marinithermus hydrothermalis |
| S116A | site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates | Marinithermus hydrothermalis |
| S279Y | site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates | Marinithermus hydrothermalis |
| T117S | site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates | Marinithermus hydrothermalis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.519 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, wild-type enzyme | Marinithermus hydrothermalis |  |
| 0.578 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, mutant S116A | Marinithermus hydrothermalis | |
| 0.887 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, mutant T117S | Marinithermus hydrothermalis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-N-acetyl-alpha-D-glucosamine | Marinithermus hydrothermalis | - |
UDP-N-acetyl-alpha-D-galactosamine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Marinithermus hydrothermalis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-termminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Marinithermus hydrothermalis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2 | Marinithermus hydrothermalis | ? | - |
? | |
| UDP-N-acetyl-alpha-D-glucosamine | - |
Marinithermus hydrothermalis | UDP-N-acetyl-alpha-D-galactosamine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | sequence comparisons and structure homology modeling, overview. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine | Marinithermus hydrothermalis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GalE | - |
Marinithermus hydrothermalis |
| UDP-Glc(NAc) 4-epimerase | - |
Marinithermus hydrothermalis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
- |
Marinithermus hydrothermalis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
half-life is 13.5 h | Marinithermus hydrothermalis |
| 60 | - |
half-life is 23 min | Marinithermus hydrothermalis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.58 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, wild-type enzyme | Marinithermus hydrothermalis | |
| 0.83 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, mutant T117S | Marinithermus hydrothermalis | |
| 1 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, mutant S116A | Marinithermus hydrothermalis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 7.5 | - |
Marinithermus hydrothermalis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9 | over 50% of maximal activity at pH 6.0 and pH 9.0 | Marinithermus hydrothermalis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | UDP-hexose 4-epimerases belong to the superfamily of short-chain dehydrogenase/reductase group 2, which typically show a two-domain structure | Marinithermus hydrothermalis |
| additional information | structure homology modeling, overview. The Marinithermus enzyme makes use of a TxnYx3K catalytic triad rather than the usual SxnYx3K triad. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine, the gatekeeper residue is responsible for the substrate specificity, the two consecutive glycine residues, Gly118 and Gly119, are a unique feature of GalE enzymes from Thermus species and important for activity as well as affinity | Marinithermus hydrothermalis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.93 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, mutant T117S | Marinithermus hydrothermalis | |
| 1.11 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, wild-type enzyme | Marinithermus hydrothermalis | |
| 1.73 | - |
UDP-N-acetyl-alpha-D-glucosamine | pH 7.5, 45°C, mutant S116A | Marinithermus hydrothermalis | |
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
