L-Glutamic acid γ-monohydroxamate has been used as a standard to calculate transglutaminase (TGase) activity.[1]
Biochem/physiol Actions
L-Glutamic acid γ-monohydroxamate [L-Glu(gamma)HXM] is used as a vanadium ligand which potentiates vanadiums metabolic activity. L-Glu(gamma)HXM is also used as a substrate for E. coli asparagine synthetase B and as an ATP-dependent irreversible inhibitor of Escherichia coli gamma-glutamylcysteine synthetase.
Bioscience, biotechnology, and biochemistry, 62(7), 1455-1457 (1998-08-28)
Incubation of Escherichia coli gamma-glutamylcysteine synthetase with L-glutamic acid gamma-monohydroxamate and ATP caused slow but irreversible inhibition of the enzyme, and more than 90% activity was lost in three days. The enzyme was not inactivated when ATP was absent or
The method for the assay of glutamine synthetase (GlnS) relies on the gamma-glutamyl transferase reaction, i.e. the formation of glutamyl-gamma-hydroxamate from glutamine and hydroxylamine, and the chromatographic separation of the reaction product from the reactants. The method is not only
Escherichia coli asparagine synthetase B (AS-B) catalyzes the synthesis of asparagine from aspartic acid and glutamine in an ATP-dependent reaction. The ability of this enzyme to employ hydroxylamine and L-glutamic acid gamma-monohydroxamate (LGH) as alternative substrates in place of ammonia
We have previously shown that L-glutamic acid gamma-monohydroxamate (GAH) exhibits an antitumor activity, both in vitro and in vivo. In this report we explore the selective cytotoxicity of GAH in vitro by comparing the survival of tumor and normal cells.
The Journal of biological chemistry, 275(34), 26233-26240 (2000-08-22)
The x-ray crystal structure of the heterodimeric carbamoyl phosphate synthetase from Escherichia coli has identified an intermolecular tunnel that connects the glutamine binding site within the small amidotransferase subunit to the two phosphorylation sites within the large synthetase subunit. The
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