Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Saccharomyces cerevisiae |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
dimer | the state is unaffected by the presence of substrate | Saccharomyces cerevisiae |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.8 | - |
assay at | Saccharomyces cerevisiae |