L. Michaelis coauthored the 1913 invertase study with Maud L. Menten. Their interpretation connected the substrate dependence of reaction speed to reversible enzyme-substrate binding followed by conversion to product. At high substrate concentration, occupation of the finite enzyme population limits the rate, giving the saturation behavior associated with Michaelis-Menten kinetics.[ref]
The Kinetics of Invertase Action by L. Michaelis and Maud L. Menten. Translated original, binding-equilibrium interpretation and the initial-rate dependence on sucrose concentration
The original equilibrium-binding argument should be distinguished from the later quasi-steady-state derivation of the same rate-law shape. Fitting that shape alone does not distinguish every possible microscopic mechanism. The Rockefeller Archive Center's identified 1946 portrait records the scientist as Leonor Michaelis.
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