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The Role of Active Site Arginines of Sorghum NADP-Malate Dehydrogenase in Thioredoxin-dependent Activation and Activity
Journal of Biological Chemistry
The activation of sorghum NADP-malate dehydrogenase is initiated by thiol/disulfide interchanges with reduced thioredoxin followed by the release of the C-terminal autoinhibitory extension and a structural modification shaping the active site into a high efficiency and high affinity for oxaloacetate conformation. In the present study, the role of the active site arginines in the activation and catalysis was investigated by sitedirected mutagenesis and arginyl-specific chemical derivatizationdoi:10.1074/jbc.m006526200 pmid:10958800 fatcat:okvcowxbqvgxlel2o63yc44jba