title: Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802-4500, USA.
authors.forename: Sarah H
authors.initials: SH
authors.lastname: Lawrence
authors.forename: James G
authors.initials: JG
authors.lastname: Ferry
mesh_terms: D001667:Binding, Competitive; D002384:Catalysis; D007700:Kinetics; D017020:Methanosarcina / Q000201:enzymology*; D010709:Phosphate Acetyltransferase / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D010709:Phosphate Acetyltransferase