Figure 2

Example enzyme kinetics data. Experimental Idh-1 kinetic data using homogenates from 1 cricket (2 legs; solid diamonds) and 2 crickets (4 legs; open squares). (A) Initial reaction velocity as a function of substrate concentration, showing the expected hyperbolic relationship. Reaction velocity increases linearly until approaching the saturation point. (B) Lineweaver-Burk plot, the double-reciprocal method for calculating K_m, the Michaelis constant, and V_max, the maximum reaction velocity, from kinetic assay data.