A New Family of <small>D</small>-2-Hydroxyacid Dehydrogenases That Comprises <small>D</small>-Mandelate Dehydrogenases and 2-Ketopantoate Reductases

Yusuke WADA; Saho IWAI; Yusuke TAMURA; Tomonori ANDO; Takeshi SHINODA; Kazuhito ARAI; Hayao TAGUCHI

doi:10.1271/bbb.70827

Biochemistry & Molecular Biology Regular Papers

A New Family of D-2-Hydroxyacid Dehydrogenases That Comprises D-Mandelate Dehydrogenases and 2-Ketopantoate Reductases

Yusuke WADA, Saho IWAI, Yusuke TAMURA, Tomonori ANDO, Takeshi SHINODA, Kazuhito ARAI, Hayao TAGUCHI

著者情報

キーワード: D-mandelate dehydrogenase, 2-ketopantoate reductase, D-2-hydroxyacid dehydrogenase, Enterococcus faecalis, Enterococcus faecium

ジャーナルフリー

2008 年 72 巻 4 号 p. 1087-1094

DOI https://doi.org/10.1271/bbb.70827

View "Advance Publication" version (April 7, 2008).

詳細

抄録

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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