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- W1640491587 abstract "The results of initial velocity studies on the 5-aminolevulinic acid synthetase reaction and product inhibition studies are consistent with an ordered bi-bi mechanism in which glycine binds to the enzyme first and 5-aminolevulinic acid dissociates last. The results are confirmed by the spectral changes of holoenzyme caused by the substrates. 5-Aminolevulinic acid synthetase activity is inhibited only by adenosine triphosphate, guanosine triphosphate and pyrophosphate. This inhibition is competitive with glycine and non-competitive with succinyl-CoA. Experiments with [α-32P]ATP, [γ-32P]ATP and [32P2]pyrophosphate have shown that adenosine triphosphate and pyrophosphate are bound on each of both forms of 5-aminolevulinic acid synthetase. The ratio is one mole per mole of enzyme. The estimation of –SH groups with 5,5′-dithiobis-(2-nitrobenzoic acid) after binding of inhibitor shows that one –SH is masked. After p-hydroxymercuribenzoate action on the enzyme, 5-aminolevulinic acid synthetase does not bind anymore [32P]ATP and is completely inactive. We suggest that ATP and pyrophosphate inhibit 5-aminolevulinic acid synthetase by acting on an –SH group of the active center of 5-aminolevulinic acid synthetase." @default.
- W1640491587 created "2016-06-24" @default.
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- W1640491587 date "1973-12-01" @default.
- W1640491587 modified "2023-09-23" @default.
- W1640491587 title "5-Aminolevulinic-Acid Synthetase of Rhodopseudomonas spheroides Y. Kinetic Mechanism and Inhibition by ATP" @default.
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- W1640491587 doi "https://doi.org/10.1111/j.1432-1033.1973.tb03164.x" @default.
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