The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.
Biochem Biophys Res Commun
; 439(1): 109-14, 2013 Sep 13.
Article
em En
| MEDLINE
| ID: mdl-23954635
ABSTRACT
D-Mandelate dehydrogenases (D-ManDHs), belonging to a new d-2-hydroxyacid dehydrogenase family, catalyze the conversion between benzoylformate and d-mandelate using NAD as a coenzyme. We determined the first D-ManDH structure, that of ManDH2 from Enterococcus faecalis IAM10071. The overall structure showed ManDH2 has a similar fold to 2-ketopantoate reductase (KPR), which catalyzes the conversion of 2-ketopantoate to d-pantoate using NADP as a coenzyme. They share conserved catalytic residues, indicating ManDH2 has the same reaction mechanism as KPR. However, ManDH2 exhibits significant structural variations in the coenzyme and substrate binding sites compared to KPR. These structural observations could explain their different coenzyme and substrate specificities.
Palavras-chave
2-Ketopantoate reductase; 2-ketopantoate reductase; 2-ketopantoate reductase from Escherichia coli; CENDH; Coenzyme specificity; Crystal structure; EcKPR; KPR; ManDH2; N-(1-d-carboxyethyl)-l-norvaline dehydrogenase from Arthrobacter sp.; Substrate specificity; d-2-HydDH; d-2-hydroxyacid dehydrogenase; d-ManDH; d-Mandelate dehydrogenase; d-mandelate dehydrogenase; d-mandelate dehydrogenase from Enterococcus faecalis IAM10071; rmsd; root mean square deviation.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Enterococcus faecalis
/
Oxirredutases do Álcool
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article