1dxy

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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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Revision as of 12:57, 30 October 2007


1dxy, resolution 1.86Å

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STRUCTURE OF D-2-HYDROXYISOCAPROATE DEHYDROGENASE

Overview

D-2-hydroxyisocaproate dehydrogenase (D-HicDH) from Lactobacillus casei is, a homodimer with 333 amino acids and a molecular mass of 37 kDa per, subunit. The enzyme belongs to the protein family of NAD+-dependent, D-2-hydroxycarboxylate dehydrogenases and within this family to the, subgroup of D-lactate dehydrogenases (D-LDHs). Compared with other D-LDHs, D-HicDH is characterized by a very low specificity regarding size and, chemical constitution of the accepted D-2-hydroxycarboxylates. Hexagonal, crystals of recombinant D-HicDH in the presence of NAD+ and, 2-oxoisocaproate (4-methyl-2-oxopentanoate) were grown with ammonium, sulphate as precipitating agent. The structure of these crystals was, solved by molecular replacement and refined to a final R-factor of 19.6%, for all measured ... [(full description)]

About this Structure

1DXY is a [Single protein] structure of sequence from [Lactobacillus casei] with SO4, NAD and COI as [ligands]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution., Dengler U, Niefind K, Kiess M, Schomburg D, J Mol Biol. 1997 Apr 4;267(3):640-60. PMID:9126843

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