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- W1481118344 abstract "A detailed kinetic investigation was made of the binding mechanism of gamma-glutamylcysteine synthetase purified from rat kidney. The results of initial rate and inhibition studies are consistent with a partially random mechanism in which ATP is the obligatory first substrate and both amino acids bind in a random order to the enzyme-ATP complex. Formation of the enzyme-substrate quaternary complex is necessary prior to release of products. This mechanism is consistent with previous binding studies with the enzyme and while it does not rule out participation of enzyme-bound gamma-glutamyl phosphate as an intermediate in catalysis, such an intermediate cannot be a discrete covalent complex." @default.
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- W1481118344 date "1976-06-01" @default.
- W1481118344 modified "2023-10-02" @default.
- W1481118344 title "The kinetic mechanism of rat kidney gamma-glutamylcysteine synthetase." @default.
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- W1481118344 doi "https://doi.org/10.1016/s0021-9258(17)33381-1" @default.
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