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Crystallization and preliminary characterization of crystals of D-2-hydroxyisocaproate dehydrogenase from
K Niefind1, H J Hecht, D Schomburg
1Gesellschaft für Biotechnologische Forschung (GBF), Molekulare und Instrumentelle Strukturforschung, Braunschweig, Germany.
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.