Protein Variants | Comment | Organism |
---|---|---|
K153M | mutation results in a 13C chemical shift of 150.8 ppm, which is 0.9 ppm downfield from that of wild-type and 1.8 ppm upfield from that of Y149F epimerase | Escherichia coli |
S124A/Y149F | mutation causes a 13C downfield perturbation of 2.8 ppm to 152.7 ppm | Escherichia coli |
Y149F | mutation results in a 13C downfield perturbation of 2.7 ppm to 152.6 ppm | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P09147 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-galactose | - |
Escherichia coli | UDP-glucose | - |
r |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | coenzyme is tightly bound at the active site. NAD+ functions as the coenzyme for the interconversion of UDP-galactose and UDP-glucose by reversibly mediating their dehydrogenation to the common intermediate UDP-4-ketohexopyranoside. NAD+ activation induced by uridine nucleotides is brought about by a conformational change of epimerase that repositions Tyr149 at an increased distance from nicotinamide N1 of NAD+ while maintaining the electrostatic repulsion between Lys153 and nicotinamide N1 of NAD+ | Escherichia coli |