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- W187013985 endingPage "117" @default.
- W187013985 startingPage "77" @default.
- W187013985 abstract "Glutamate dehydrogenases, as a class, catalyze the reversible oxidative deamination of L-glutamate to α-ketoglutarate and ammonia. The description of the characteristics of this reaction from a variety of sources show that, although all classed as glutamate dehydrogenase, the enzymes are different in terms of kinetic characteristics, metabolic function, and molecular properties. The animal enzymes are sensitive to the concentration of purine nucleotides, can catalyze the reaction using either Nicotinamide adenine dinucleotide (NAD) or Nicotinamide adenine dinucleotide phosphate (NADP), and undergo a reversible polymerization reaction, which might influence the allosteric characteristics of the enzyme. The non-animal sources are specific either for NAD or for NADP, are in general not influenced by purine nucleotides, and do not appear to undergo a reversible polymerization reaction. These differences are related to the metabolic role of the reaction, which in animal tissues serves as an important link between carbohydrate and protein metabolism utilizing either α-ketoglutarate or glutamate depending on the condition of the cell, but which in non-animal organisms might act unidirectionally." @default.
- W187013985 created "2016-06-24" @default.
- W187013985 creator A5035055956 @default.
- W187013985 creator A5043445006 @default.
- W187013985 date "1971-01-01" @default.
- W187013985 modified "2023-10-09" @default.
- W187013985 title "L-Glutamate Dehydrogenases* *Research work cited in this review which originates in the author's laboratory was supported in part by research grant AM 13332, United States Public Health Service and research grant GB 26583X from the National Science Foundation." @default.
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