Abstract
The initial velocity, product inhibition, and isotopic exchange data show that the substrates of bovine heart mitochondrial acetyl-CoA synthetase add to the enzyme in an ordered fashion, with MgATP adding first followed by the addition of acetate, then the release of MgPPi immediately before the addition of CoA.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 537-542 |
| Number of pages | 6 |
| Journal | International Journal of Biochemistry |
| Volume | 6 |
| Issue number | 8 |
| DOIs | |
| State | Published - Jan 1 1975 |
ASJC Scopus subject areas
- Biochemistry
Fingerprint Dive into the research topics of 'Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates'. Together they form a unique fingerprint.
Cite this
Farrar, W. W., & Plowman, K. (1975). Kinetics of acetyl-CoA synthetase-I. Mode of addition of substrates. International Journal of Biochemistry, 6(8), 537-542. https://doi.org/10.1016/0020-711X(75)90069-5