title: On the generality of Michaelian kinetics.
abstract: The reversible Michaelis-Menten equation is shown to follow from a very broad class of steady-state kinetic models involving enzymes that adopt a unique free (i.e., not complexed to substrate/product) state in solution. In the case of enzymes with multiple free states/conformations (e.g., fluctuating, hysteretic, or co-operative monomeric enzymes), Michaelian behavior is still assured if the relative steady-state populations of free enzyme states are independent of substrate and product concentration. Prior models for Michaelian behavior in multiple conformer enzymes are shown to be special cases of this single condition.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA and Department of Physics, University of California, Santa Barbara, California 93106, USA.
authors.forename: Itay
authors.initials: I
authors.lastname: Barel
authors.affiliation: Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA and Department of Physics, University of California, Santa Barbara, California 93106, USA.
authors.forename: Frank L H
authors.initials: FL
authors.lastname: Brown
mesh_terms: D004798:Enzymes / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008956:Models, Chemical
chemical_list: D004798:Enzymes