TY - JOUR T1 - Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from thermus thermophilus JF - Acta Crystallographica Section F-Structural Biology and Crystallization Communications Y1 - 2010 A1 - Merli, Angelo A1 - Manikandan, Karuppasamy A1 - Graczer, Eva A1 - Schuldt, Linda A1 - Singh, Rajesh Kumar A1 - Zavodszky, Peter A1 - Vas, Maria A1 - Weiss, Manfred S. AB -

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 Mg(2+) or Mn(2+) 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.

PB - WILEY-BLACKWELL PUBLISHING, INC CY - COMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USA VL - 66 U3 - Foreign U4 - 0.563 ER -