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Plant Physiology 49:87-90 (1972)
© 1972 American Society of Plant Biologists

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Articles

Glutamate Dehydrogenase from Apodachlya (Oomycetes) 1

Jeffrey S. Price2 and Frank H. Gleason

a Department of Biology, The Colorado College, Colorado Springs, Colorado 80903

A glutamate dehydrogenase specific for nicotinamide-adenine-dinucleotide has been purified 50-fold from Apodachlya brachynema (Leptomitales). Certain physical, chemical, and kinetic properties of this enzyme have been studied, particularly specificity for coenzymes and substrates. With glucose as the sole carbon source, the synthesis of glutamate dehydrogenase was repressed, whereas glutamate, proline, alanine, or ornithine plus aspartate as sole carbon sources induced synthesis of the enzyme. These data indicate that the function of this enzyme is primarily degradative, although there is no evidence for a nicotinamide-adenine-dinucleotide-phosphate-specific biosynthetic glutamate dehydrogenase in Apodachlya.

2 Present address: Department of Biology, Rice University, Houston, Texas 77001.

1 This study was supported by a grant from the Milheim Foundation and by funds from the Department of Biology, The Colorado College, for undergraduate research.






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Copyright © 1972 by the American Society of Plant Biologists