干酪乳杆菌D-2-羟基异己酸脱氢酶晶体的结晶及初步表征

Crystallization and preliminary characterization of crystals of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei.

作者信息

Niefind K, Hecht H J, Schomburg D

机构信息

Gesellschaft für Biotechnologische Forschung (GBF), Molekulare und Instrumentelle Strukturforschung, Braunschweig, Germany.

出版信息

J Mol Biol. 1994 Jul 22;240(4):400-2. doi: 10.1006/jmbi.1994.1454.

DOI:10.1006/jmbi.1994.1454

PMID:8035463

Abstract

D-2-hydroxyisocaproate dehydrogenase (D-HicDH) from Lactobacillus casei is a homodimeric enzyme with a molecular mass of 74.6 kDa. It catalyzes the reduction of a wide range of 2-ketocarboxylic acids to D-2-hydroxycarboxylic acids using NADH as co-substrate. The enzyme has been crystallized by vapor diffusion using ammonium sulfate as precipitant. The crystals belong to hexagonal space group type P6(3)22 with a = b = 134.1 A, c = 124.1 A and diffract X-rays to 3.0 A resolution. Packing considerations show that there are either one or two D-HicDH monomers in the asymmetric unit.

摘要

来自干酪乳杆菌的D-2-羟基异己酸脱氢酶（D-HicDH）是一种同型二聚体酶，分子量为74.6 kDa。它以NADH作为共底物，催化多种2-酮羧酸还原为D-2-羟基羧酸。该酶已通过以硫酸铵为沉淀剂的气相扩散法结晶。晶体属于六方空间群P6(3)22，a = b = 134.1 Å，c = 124.1 Å，X射线衍射分辨率为3.0 Å。堆积分析表明，不对称单元中存在一个或两个D-HicDH单体。