Prasad P V, Hatefi Y
Biochemistry. 1986 May 6;25(9):2459-64. doi: 10.1021/bi00357a025.
Data presented in this paper suggest that D-(-)-beta-hydroxybutyrate dehydrogenase (BDH) purified from bovine heart mitochondria contains an essential carboxyl group and an essential histidyl residue at or near the active site. Lactate and malate dehydrogenases, which catalyze reactions analogous to that catalyzed by BDH, also contain an aspartyl and a histidyl residue at the active site [Birktoft, J.J., & Banaszak, L.J. (1983) J. Biol. Chem. 258, 472-482]. In addition, all three enzymes contain an essential arginyl residue, apparently concerned with electrostatic interaction with their respective carboxylic acid substrates, and promote ternary adduct formation involving the enzyme, NAD, and sulfite.
本文中呈现的数据表明，从牛心线粒体中纯化得到的D-(-)-β-羟基丁酸脱氢酶（BDH）在活性位点处或其附近含有一个必需的羧基和一个必需的组氨酸残基。催化与BDH所催化反应类似反应的乳酸脱氢酶和苹果酸脱氢酶，在活性位点也含有一个天冬氨酰残基和一个组氨酸残基[伯克托夫特，J.J.，& 巴纳扎克，L.J.（1983年）《生物化学杂志》258卷，472 - 482页]。此外，这三种酶都含有一个必需的精氨酰残基，显然与它们各自的羧酸底物的静电相互作用有关，并促进涉及酶、NAD和亚硫酸盐的三元加合物的形成。
