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