The nonallosteric mechanism of enzyme activity regulation. Is it the only true mechanism?
The nonallosteric regulation mechanism of enzyme reaction velocity assumes that the substrate and enzyme interact via a metal cation and form simple and mixed, mono- and multi-nuclear complexes. A solution of equations for individual cases gives a function of initial reaction velocity at any given substrate or modifier concentration. This function can describe kinetic effects that are considered allosteric, as well as phenomena omitted by commonly-accepted models.
Kuczek
Marian
M
Department of Experimental and Applied Biology, University of Opole, Kominka 4, Poland. kuczek@uni.opole.pl
D000494:Allosteric Regulation; D004798:Enzymes / Q000378:metabolism*; D005246:Feedback; D007700:Kinetics; D008954:Models, Biological; D011770:Pyruvate Kinase / Q000378:metabolism
D004798:Enzymes; D011770:Pyruvate Kinase