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 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.
Merli
Angelo
A
Department of Biochemistry and Molecular Biology, University of Parma, Viale G. P. Usberti 23/A, 43100 Parma, Italy.
Manikandan
Karuppasamy
K
Gráczer
Eva
E
Schuldt
Linda
L
Singh
Rajesh Kumar
RK
Závodszky
Péter
P
Vas
Mária
M
Weiss
Manfred S
MS
D050539:3-Isopropylmalate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D013379:Substrate Specificity; D016963:Thermus thermophilus / Q000201:enzymology*
D050539:3-Isopropylmalate Dehydrogenase