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Literature summary for 1.1.1.345 extracted from

  • Miyanaga, A.; Fujisawa, S.; Furukawa, N.; Arai, K.; Nakajima, M.; Taguchi, H.
    The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase (2013), Biochem. Biophys. Res. Commun., 439, 109-114.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Enterococcus faecium

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are grown from a 1:1 mixture of a protein solution (10 mg/ml in 10 mM Tris–HCl (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

Protein Variants Comment Organism
K187A mutant has completely lost its activity Enterococcus faecium

Organism

Organism UniProt Comment Textmining
Enterococcus faecium E3USM3
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-

Purification (Commentary)

Purification (Comment) Organism
-
Enterococcus faecium

Synonyms

Synonyms Comment Organism
D-mandelate dehydrogenase misleading Enterococcus faecium
ManDH2
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Enterococcus faecium