| Literature DB >> 16428419 |
Sarah H Lawrence1, James G Ferry.
Abstract
Phosphotransacetylase (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.Entities:
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Year: 2006 PMID: 16428419 PMCID: PMC1347351 DOI: 10.1128/JB.188.3.1155-1158.2006
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490