Introducing Quantitative Assessment of Michaelis Constant (K_m) Accuracy.

ABSTRACT: The Michaelis constant (K_m) is central to enzyme kinetics, guiding variant selection, inhibitor screening, and metabolic modeling. However, K_m obtained by nonlinear regression can be substantially inaccurate even when the reported standard error (SE) appears small. Common software reports SE but provides no accuracy metric. This gap is addressed by extending the accuracy confidence interval (ACI) framework to K_m (ACI-K_m) through a binding-isotherm formulation of the velocity-substrate fit. Given confidence intervals for concentration accuracy, the method quantifies how residual systematic uncertainties in enzyme and substrate concentrations ( E₀ and S₀) propagate into the determined K_m values and provides a probab

SUBMITTER: Wang TY 

PROVIDER: S-EPMC12703444 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature