Kinetics of acetyl-CoA synthetase-II. Product inhibition studies
- William W. Farrar(corresponding author),
- Kent M. Plowman
- Virginia Polytechnic Institute and State University,
Open access
Abstract
Product inhibition studies with bovine heart mitochondrial acetyl-CoA synthetase yielded the following results: 1. 1. Uncompetitive inhibition by AMP, and noncompetitive inhibition by acetyl-CoA as product inhibitors, both with CoA as the variable substrate. 2. 2. Competitive inhibition by both AMP and acetyl-CoA as product inhibitors with either acetate or MgATP as the variable substrate. The uncompetitive inhibition by AMP with CoA as the variable substrate, and the competitive inhibitions by AMP and acetyl-CoA with either MgATP or acetate as variable substrate can perhaps be reconciled by a model in which AMP induces randomness in the addition of MgATP and acetate, but not the release of acetyl-CoA and AMP, while acetyl-CoA induces randomness in both the addition and release of these substrates and products.
Publication Information
Output type
Original language
English (US)Pages from-to (Number of pages)
Pages 583-588 (6 pages)Journal (Volume, Issue Number)
International Journal of Biochemistry (Volume 10, Issue 7)Publication milestones
- Published - 1979
Publication status
ISSN
0020-711XPublication IDs
- Scopus: 0018370382
- PubMed: 38154
