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- W2034951635 abstract "Glutamine synthetase which catalyzes the conversion of l-glutamate to glutamylhydroxamate in the presence of hydroxylamine and to l-glutamine in the presence of ammonia was purified 20-fold from extracts of Lactobacillus arabinosus. The properties of the enzyme were found to differ in several respects from the glutamine synthetases derived from other sources. The glutamine synthetase of L. arabinosus does not utilize d-glutamate and does not catalyze a glutamyl transfer reaction. The production of glutamine synthetase in L. arabinosus is decreased more than 6-fold when the cells are grown in the presence of l-glutamine. In addition, the activity of the glutamine synthetase is inhibited in vitro by l-glutamine, and the inhibition appears to be competitive with all of the substrates, l-glutamate, hydroxylamine, ammonia, and ATP. The Ki value for l-glutamine is 10- and 20-fold lower than the Km values for l-glutamate and ammonia, respectively, indicating the l-glutamine is more tightly bound to the enzyme than either l-glutamate or ammonia." @default.
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- W2034951635 date "1965-09-01" @default.
- W2034951635 modified "2023-10-10" @default.
- W2034951635 title "Control of glutamine synthesis in Lactobacillus arabinosus" @default.
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- W2034951635 doi "https://doi.org/10.1016/0003-9861(65)90255-9" @default.
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