Abstract
Isotope exchange at equilibrium has been used to study the kinetic mechanism of the choline acetyltransferase reaction. The choline-acetylcholine, acetyl-CoA-acetylcholine, and CoA-acetyl-CoA exchange patterns are qualitatively consistent with a Theorell-Chance mechanism. However, quantitative differences are observed when the experimental results are compared to theoretical fits of the data for a Theorell-Chance mechanism. It is concluded that the kinetic mechanism of the choline acetyltransferase reaction can best be described as a random Theorell-Chance mechanism in which a low but finite amount of ternary complex exists.
| Original language | English |
|---|---|
| Pages (from-to) | 12820-12825 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 257 |
| Issue number | 21 |
| State | Published - Nov 10 1982 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology