Crystallization and preliminary characterization of crystals of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei.
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.
Gesellschaft für Biotechnologische Forschung (GBF), Molekulare und Instrumentelle Strukturforschung, Braunschweig, Germany.
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Niefind
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Hecht
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Schomburg
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D013379:Substrate Specificity
D000429:Alcohol Oxidoreductases; C047961:2-hydroxyisocaproate dehydrogenase