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- W2085686147 abstract "The inhibition of Escherichia coli glutamine synthetase by phosphinothricin [2-amino-4-(methylphosphinyl)butanoic acid] has been studied. This amino acid was observed to function as an active site directed inhibitor exhibiting time-dependent inhibition of glutamine synthetase in the presence of ATP or adenylylimidodiphosphate (AMPPNP) but not adenylyl(β,γ-methylene) diphosphonate (AMPPCP). The inactivation was observed to be pseudo-first order. Phosphinothricin was also found to inhibit the enzyme reversibly under initial rate conditions and was competitive with respect to glutamate with K1S = 18 ± 3 μm. The inactive enzyme inhibitor complex was found to contain approximately 11 molecules of ADP and of 32P per dodecamer using [γ-32P]ATP. Reactivation of the inactive enzyme complex was achieved by incubating the enzyme complex in 50 mm acetate (pH 4.4), 1 m KCl, and 0.40 m (NH4)2SO4. ADP, phosphinothricin, and Pi were released upon reactivation." @default.
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- W2085686147 date "1986-06-01" @default.
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- W2085686147 title "Inhibition of Escherichia coli glutamine synthetase by phosphinothricin" @default.
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- W2085686147 doi "https://doi.org/10.1016/0045-2068(86)90026-x" @default.
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