NITROGEN ASSIMILATION IN MYCORRHIZAS. I. PURIFICATION AND PROPERTIES OF THE NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE-SPECIFIC GLUTAMATE DEHYDROGENASE OF THE ECTOMYCORRHIZAL FUNGUS CENOCOCCUM GRANIFORME
Article first published online: 2 MAY 2006
Volume 93, Issue 3, pages 415–422, March 1983
How to Cite
MARTIN, F., MSATEF, Y. and BOTTON, B. (1983), NITROGEN ASSIMILATION IN MYCORRHIZAS. I. PURIFICATION AND PROPERTIES OF THE NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE-SPECIFIC GLUTAMATE DEHYDROGENASE OF THE ECTOMYCORRHIZAL FUNGUS CENOCOCCUM GRANIFORME. New Phytologist, 93: 415–422. doi: 10.1111/j.1469-8137.1983.tb03441.x
- Issue published online: 2 MAY 2006
- Article first published online: 2 MAY 2006
- (Accepted 19 September 1982)
The nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase (L-gluta-mate: NADP+ oxido-reductase, ECI .4.1 .4) of the ectomycorrhizal Ascomycete Cenococcum graniforme was purified twofold to electrophoretic homogeneity. The native enzyme was shown to have a molecular weight of 320000 and to be composed of six identical subunits with a molecular weight of 48 000. The pH optimum for the animating reaction was 7.6 NADP-GDH showed a negative co-operativity with respect to ammonia (Km1:2mM, Km2:8 mM). The Km values for α-ketoglutarate and NADPH were 2 mM and 0.03 mM, respectively. The physical and kinetics properties of this enzyme are similar with those reported for NADP-GDH of other fungi.
Cross-reactivity of a rabbit monospecific antiserum raised against the NADP-GDH from Sphaerostilbe repens, a saprophytic Ascomycete, was tested against the enzyme of C. graniforme. The immunochemical homology of both enzymes are low suggesting that a substitution occurs in amino acid residue of the protein.