Abstract
Phospliotransacetylase (EC 2.3.1.8) catalyzes the reversible transfer of the acetyl group from acetyl phosphate to coenzyme A (CoA), forming acetyl-CoA and inorganic phosphate. A steady-state kinetic analysis of the phosphotransacetylase from Methanosarcina thermophila indicated that there is a ternary complex kinetic mechanism rather than a ping-pong kinetic mechanism. Additionally, inhibition patterns of products and a nonreactive substrate analog suggested that the substrates bind to the enzyme in a random order. Dynamic light scattering revealed that the enzyme is dimeric in solution.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1155-1158 |
| Number of pages | 4 |
| Journal | Journal of bacteriology |
| Volume | 188 |
| Issue number | 3 |
| DOIs | |
| State | Published - Feb 2006 |
All Science Journal Classification (ASJC) codes
- Microbiology
- Molecular Biology