title: Kinetic properties of soluble adenosine triphosphatase of Escherichia coli.
abstract: Bound and solubilized ATPase from Escherichia coli show similar kinetic properties. The saturation curves for MgATP are hyperbolic with both preparations. The straight lines in the Line-weaver-Burk plot indicate that MgATP is the true substrate, that one molecule MgATP is bound per enzyme molecule, and that there is no cooperativity. Presence of EDTA leads to sigmoidal saturation curves. This effect could be reversed by adding MgCl2 stoichiometrically to EDTA. Different results in other publications, especially in that of CARREIRA and MUNOZ1 can be explained as being primarily the consequence of complexing agent contaminations in the assay.
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism
chemical_list: D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D008274:Magnesium