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• W2161011670 abstract "Abstract Substrate concentration effects on isotopic exchange rates at equilibrium have been measured with Escherichia coli glutamate synthetase (adenylated form) with 32P, 14C, 18O, and 15N. A new test for possible compulsory substrate-binding orders is presented, involving measurement of equilibrium exchange rates while increasing concentration of all substrates. This test shows random substrate-binding patterns for the enzyme. Inhibition of some equilibrium exchange rates while various pairs of substrates were increased in concentration appears to result from competitive rather than compulsory binding order effects. The relative rates of equilibrium exchanges were (glutamate ⇄ glutamine) g (NH3 ⇄ glutamine) g (Pi ⇄ ATP) = (ADP ⇄ ATP). The inequalities show that interconversion of bound substrates is not the only rate-limiting step, and allow deductions about relative association-dissociation rates of various substrates. Glutamine synthetase from E. coli does not catalyze any detectable ADP ⇄ ATP, Pi ⇄ ATP, glutamate ⇄ glutamine, or NH3 ⇄ glutamine exchanges unless all substrates are present. The absence of ADP ⇄ ATP exchange in presence of glutamate or of NH3 ⇄ glutamine exchange in presence of Pi, together with lack of compulsory substrate-binding orders, does not give support to formation of γ-glutamyl phosphate as an enzyme-bound intermediate. No phosphoryl enzyme, glutamyl enzyme, or amido enzyme could be detected by isotopic labeling and isolation procedures. The results suggest further consideration of a concerted reaction mechanism requiring all substrates present in the active site." @default.
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• W2161011670 date "1972-02-01" @default.
• W2161011670 modified "2023-10-17" @default.
• W2161011670 title "Substrate Binding and Reaction Intermediates of Glutamine Synthetase (Escherichia coli W) as Studied by Isotope Exchanges" @default.
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• W2161011670 doi "https://doi.org/10.1016/s0021-9258(19)45606-8" @default.
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