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Activation of an nadph oxidase from maize by dipicolinic acid
Affiliation:1. Department of Botany and Department of Environmental Practice University of Tennessee Knoxville, TN 37996, U.S.A.;1. Department of Neurosurgery, National Institute of Mental Health and Neurosciences, Bangalore, India;2. Department of Neuropathology, National Institute of Mental Health and Neurosciences, Bangalore, India;1. Department of Biology, Faculty of Sciences of the University of Porto, Rua do Campo Alegre s/n, 4169-007, Porto, Portugal;2. INOV4Agro - GreenUPorto - Research Centre on Sustainable Agri-Food Production, Department of Biology, Faculty of Sciences of the University of Porto, Rua do Campo Alegre s/n, 4169-007, Porto, Portugal;3. LAQV/REQUIMTE, Department of Biology, Faculty of Sciences of the University of Porto, Rua do Campo Alegre s/n, 4169-007, Porto, Portugal;1. Graduate School of Agriculture, Forestry and Fisheries, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan;2. Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan;3. The United Graduate School of Agricultural Sciences, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan;4. Setsunan University, 45-1 Nagaotoge, Hirakata, Osaka, 573-0101, Japan;5. Kenya Plant Health Inspectorate Service, Nairobi, Kenya;6. National Agricultural Research Organization, Abi Zonal Agricultural Research and Development Institute, Plot 3, Lugard Avenue P.O. Box 295, Entebbe, Uganda
Abstract:An NADPH oxidase has been partially purified from maize kernels. The activity of this enzyme, as measured by NADPH disappearance or oxygen consumption, was enhanced by dipicolinic acid (pyridine 2,6-dicarboxylic acid). Dipicolinic acid was not consumed in this reaction indicating that it was an activator rather than a substrate of this enzyme.
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