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- W1980892580 abstract "Abstract Decarboxylation of pyruvic acid by the pyruvic carboxylase of yeast, follows firstorder kinetics until the reaction is virtually complete in any specific solution of enzyme and substrate, but the velocity constant changes, increasing slightly then decreasing, as the initial substrate concentration is increased. If the substrate concentration is allowed to decrease, during the reaction, to about half its initial value, and then is restored to the original value by addition of more substrate, the rate constant immediately decreases to approximately the value it would have had if all the substrate had been added at once. This cannot be due to competition between substrate molecules as in excess substrate inhibition. The rate constant appears to be set by the initial concentration of substrate and to be unaffected by subsequent changes in it, except addition of more substrate. The bearing of this on enzyme kinetic theory is discussed." @default.
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- W1980892580 date "1961-04-01" @default.
- W1980892580 modified "2023-09-27" @default.
- W1980892580 title "Studies of enzyme kinetics. I. The course of the reaction and the effect of a second addition of substrate on pyruvic carboxyiase of yeast" @default.
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- W1980892580 doi "https://doi.org/10.1016/0003-9861(61)90312-5" @default.
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