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PMID: 6221721 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Re-assessment of ammonium-ion affinities of NADP-specific glutamate dehydrogenases. Activation of the Neurospora crassa enzyme by ammonium and rubidium ions.

The Biochemical journal ·Vol. 209 ·No. 2 ·1983-02-01 ·Pages 527-31

Wootton JC

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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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1983-02-01
Pages
527-31
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1154121
Subset
IM
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