Open AccessGlutamate Dehydrogenase from Apodachlya (Oomycetes)
Author(s) -
Jeffrey S. Price,
Frank H. Gleason
Publication year - 1972
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.49.1.87
Subject(s) - glutamate dehydrogenase , biochemistry , nicotinamide adenine dinucleotide , cofactor , enzyme , glutamate synthase , nicotinamide adenine dinucleotide phosphate , dehydrogenase , glutamate receptor , alanine , nad+ kinase , nicotinamide , branched chain alpha keto acid dehydrogenase complex , chemistry , biology , amino acid , oxidase test , receptor
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.