Abstract
Cell-free extracts of M. pyogenes var. aureus and a number of other bacteria catalyse the synthesis of glutamylhydroxamic acid from glutamic acid and hydroxylamine in the presence of adenosine triphosphate (ATP) and Mg. Glutamine is synthesized when hydroxylamine is replaced by ammonia. Synthesis of glutamine and glutamylhydroxamic acid is accompanied by the appearance of an equivalent amount of phosphate. The enzyme system is activated by optimum concentrations of Mn as effectively as by Mg. Synthesis is inhibited by Ca, Na fluoride, ATP, para-chloromercuribenzoate and methionine sulphozide. Na fluoride is more effective in the presence of Mg than in the presence of Mn.