Abstract
Ultraviolet differential spectroscopic measurements show the existence of a glutamate dehydrogenase ( l-glutamate:NAD(P) + oxidoreductase (deaminating), EC 1.4.1.3)— l-glutamate complex. The spectral features resemble perturbation difference spectra of enzyme aromatic amino acid chromophores and allow the determination of the l-glutamate concentration dependence. The dissociation constant for this enzyme- l-glutamate complex was approximately 48 mM and was independent of enzyme concentration. The lack of interaction between the binding of l-glutamate and the activating monocarboxylic amino acids indicates that they bind at totally separate sites.
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