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Literature summary for 5.1.3.3 extracted from
- Characterization of the Saccharomyces cerevisiae galactose mutarotase/UDP-galactose 4-epimerase protein, Gal10p (2007), FEMS Yeast Res., 7, 366-371.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharomyces cerevisiae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics of the epimerase reaction, recombinant enzyme | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-galactose | Saccharomyces cerevisiae | the two enzyme activities, galactose mutarotase and UDP-galactose 4-epimerase, are required for the Leloir pathway of D-galactose catabolism, they are contained within a single proteinGal10p | beta-D-galactose | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
galactose is the preferred substrate, overview, coupled assay using glucose/galactose dehydrogenase from Thermoplasma acidophilum specific for the beta-forms of D-glucose and D-galactose, and requiring NADP+ as a cofactor | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-D-galactose | the two enzyme activities, galactose mutarotase and UDP-galactose 4-epimerase, are required for the Leloir pathway of D-galactose catabolism, they are contained within a single proteinGal10p | Saccharomyces cerevisiae | beta-D-galactose | - |
? | |
| alpha-D-galactose | the simultaneous epimerase and the mutarotase activities of the bifunctional enzyme do not affect each other, the mutarotase active site has a strong preference for galactose over glucose, overview | Saccharomyces cerevisiae | beta-D-galactose | - |
? | |
| alpha-D-glucose | the simultaneous epimerase and the mutarotase activities of the bifunctional enzyme do not affect each other, the mutarotase active site has a strong preference for galactose over glucose, overview | Saccharomyces cerevisiae | beta-D-glucose | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | the state is unaffected by the presence of substrate | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aldose 1-epimerase | - |
Saccharomyces cerevisiae |
| Gal10p | - |
Saccharomyces cerevisiae |
| galactose mutarotase | - |
Saccharomyces cerevisiae |
| galactose mutarotase/UDP-galactose 4-epimerase protein | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.8 | - |
assay at | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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