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Crystallization and preliminary X‐ray diffraction analysis of various enzyme–substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus

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The Thermus thermophilus 3‐isopropylmalate dehydrogenase (Tt‐IPMDH) enzyme catalyses the penultimate step of the leucine‐biosynthesis pathway. It converts (2R,3S)‐3‐isopropylmalate to (2S)‐2‐isopropyl‐3‐oxosuccinate in the presence of divalent Mg2+ or Mn2+ and with the help of NAD+. In order to elucidate the detailed structural and functional mode of the enzymatic reaction, crystals of Tt‐IPMDH were grown in the presence of various combinations of substrate and/or cofactors. Here, the crystallization, data collection and preliminary crystallographic analyses of six such complexes are reported.
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Keywords: Thermus thermophilus; isopropylmalate dehydrogenase; leucine‐biosynthesis pathway

Document Type: Research Article

Publication date: June 1, 2010

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