Glutamate dehydrogenase from apodachlya (oomycetes).

Plant Physiol

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

Published: January 1972

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.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC365905PMC
http://dx.doi.org/10.1104/pp.49.1.87DOI Listing

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