Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Enterococcus faecium |
Crystallization (Comment) | Organism |
---|---|
crystals are grown from a 1:1 mixture of a protein solution (10 mg/ml in 10 mM TrisHCl (pH 7.5)) and a reservoir solution (0.085 M HEPES-Na (pH 7.5), 0.17 M ammonium acetate and 22.5% PEG8000) using the hanging-drop vapor diffusion method at 25°C. The overall structure shows that the enzyme has a similar fold to 2-ketopantoate reductase, which catalyzes the conversion of 2-ketopantoate to D-pantoate using NADP+ as a coenzyme. They share conserved catalytic residues, indicating that D-mandelate dehydrogenase ManDH2 has the same reaction mechanism as 2-ketopantoate reductase. However, D-mandelate dehydrogenase ManDH2 exhibits significant structural variations in the coenzyme and substrate binding sites compared to 2-ketopantoate reductase. These structural observations can explain their different coenzyme and substrate specificities | Enterococcus faecium |
Protein Variants | Comment | Organism |
---|---|---|
K187A | mutant has completely lost its activity | Enterococcus faecium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Enterococcus faecium | E3USM3 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Enterococcus faecium |
Synonyms | Comment | Organism |
---|---|---|
D-mandelate dehydrogenase | misleading | Enterococcus faecium |
ManDH2 | - |
Enterococcus faecium |