一个新的D-2-羟基酸脱氢酶家族，包括D-扁桃酸脱氢酶和2-酮泛酸还原酶。
A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases.
作者信息
Wada Yusuke, Iwai Saho, Tamura Yusuke, Ando Tomonori, Shinoda Takeshi, Arai Kazuhito, Taguchi Hayao
机构信息
Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510, Japan.
出版信息
Biosci Biotechnol Biochem. 2008 Apr;72(4):1087-94. doi: 10.1271/bbb.70827. Epub 2008 Apr 7.
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.
通过活性染色法和聚合酶链反应（PCR）分离出粪肠球菌IAM10071的D-扁桃酸脱氢酶（D-ManDH）基因，并在大肠杆菌细胞中进行表达。重组酶对具有庞大疏水侧链的各种2-酮酸底物表现出高催化活性，特别是对诸如苯甲酰甲酸和2-酮异戊酸等C3分支底物，并且对NADH和NAD(+)具有严格的辅酶特异性。它与已知依赖NADP的2-酮泛酸还原酶（KPR）表现出显著的序列相似性。这些结果表明，D-ManDH与KPR一起构成了一个新的D-2-羟基酸脱氢酶家族，该家族作用于对辅酶和底物具有各种特异性的C3分支2-酮酸底物。
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