Abstract
The NADP-specific glutamate dehydrogenase of Neurospora crassa shows complex interactions with NH4+ ions, characterized by biphasic downwardly convex double-reciprocal plots. These kinetics are explained by the action of NH4+ both as a substrate and, acting at a separate cation-binding site, as an activator. Rb+ ions, and to a smaller extent other univalent cations, also activate by acting as analogues of NH4+. Previous failure to recognize this effect, which probably also occurs in homologous enzymes from some other species, has led to significant overestimates in published reports of the Km for NH4+ of some NADP-specific glutamate dehydrogenases.
MeSH Terms
Ammonium Chloride/pharmacology
Cations/pharmacology
Chlorella/enzymology
Enzyme Activation/drug effects
Glutamate Dehydrogenase/metabolism
Kinetics
NADP/pharmacology
Neurospora/enzymology
Neurospora crassa/enzymology
Rubidium/pharmacology
Chemicals
Cations
Ammonium Chloride
NADP
Glutamate Dehydrogenase
Rubidium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Wootton J C
References (16)
16 references, click to expand
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