Lysine and tyrosine in the NADH inhibitory site of bovine liver glutamate dehydrogenase

Lysine and tyrosine in the NADH inhibitory site of bovine liver glutamate dehydrogenase

Native glutamate dehydrogenase is inhibited by high concentrations of NADH by binding at a regulatory site distinct from the catalytic site. It is concluded that both tyrosine and lysine are present in the NADH inhibitory site, and that covalent modification of either residue of the catalytically ac...

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Veröffentlicht in:The Journal of biological chemistry 1981-11, Vol.256 (22), p.11866-11872
Hauptverfasser: Saradambal, K V, Bednar, R A, Colman, R F
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine - analogs & derivatives
Adenosine - pharmacology
Amino Acids - analysis
Animals
Binding Sites
Cattle
glutamate dehydrogenase (NAD(P) super(+))
Glutamate Dehydrogenase - antagonists & inhibitors
Kinetics
liver
Liver - enzymology
Lysine
NAD - pharmacology
NADH
Oxidation-Reduction
Protein Binding
Tyrosine
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Beschreibung
Zusammenfassung:Native glutamate dehydrogenase is inhibited by high concentrations of NADH by binding at a regulatory site distinct from the catalytic site. It is concluded that both tyrosine and lysine are present in the NADH inhibitory site, and that covalent modification of either residue of the catalytically active hexameric enzyme is sufficient to eliminate NADH inhibition.
ISSN:0021-9258
DOI:10.1016/S0021-9258(19)68486-3