A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases.
Biosci Biotechnol Biochem
; 72(4): 1087-94, 2008 Apr.
Article
em En
| MEDLINE
| ID: mdl-18391442
ABSTRACT
The gene for the D-mandelate dehydrogenase (D-ManDH) of Enterococcus faecalis IAM10071 was isolated by means of an activity staining procedure and PCR and expressed in Escherichia coli cells. The recombinant enzyme exhibited high catalytic activity toward various 2-ketoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-ketoisovalerate, and strict coenzyme specificity for NADH and NAD(+). It showed marked sequence similarity with known NADP-dependent 2-ketopantoate reductases (KPR). These results indicate that together with KPR, D-ManDH constitutes a new family of D-2-hydroxyacid dehydrogenases that act on C3-branched 2-ketoacid substrates with various specificities for coenzymes and substrates.
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Base de dados:
MEDLINE
Assunto principal:
Enterococcus faecalis
/
Oxirredutases do Álcool
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article