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Crystallization and preliminary X-ray analysis of α-­isopropylmalate synthase from Mycobacterium tuberculosis

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α-Isopropylmalate synthase catalyses the aldol condensation of α-­ketoisovalerate and acetyl coenzyme A to produce α-isopropylmalate. This reaction is the first committed step of leucine biosynthesis, which is interrelated with the pathways for production of the other branched-chain amino acids, valine and isoleucine. The absence of these pathways in mammals suggests that these enzymes could be useful targets for drug design against microbial pathogens. The gene for α-IPMS in Mycobacterium tuberculosis (Rv3710) has been cloned, expressed in Escherichia coli, both in native and selenomethionine-substituted forms, and crystallized. The SeMet crystals are suitable for high-resolution X-ray structural analysis. These crystals are monoclinic, with unit-cell parameters a = 54.25, b = 154.73, c = 68.82 Å, space group P21 and two molecules in the asymmetric unit. X-ray diffraction data to 2.0 Å resolution have been collected.

Keywords: branched-chain amino-acid biosynthesis; structural genomics; tuberculosis; α-isopropylmalate synthase

Document Type: Research Article


Publication date: June 1, 2004


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