The 4 graphs above represent the change in enzyme kinetics with the individual addition of different compounds that could be categorized as either: allosteric inhibitors, allosteric activators, competitive inhibitors, activators or non-competitive inhibitors.
Enzymes kinetics - is the study of the rate of reaction of enzyme catalyzed reactions. The reaction rate is measured with effects of varying substrate concentrations and also varying the other conditions like temp, pH, effect of inhibitors and activators.
Michaelis Menten kinetics curve is the representation of Substate concentration vs reaction rate which is based on Michaelis Menten equation and rectangular hyperbolic graph. Non-linearity of Michaelis Menten kinetics curve makes the estimation of Vmax and Km difficult, thus, researchers modified the Michaelis Menten equation and developed linear graph in Lineweaver Burk plot for accurate calculation of Km and Vmax.
Vmax is the maximum velocity of chemicals reaction and Km is the substrate concentration at which half of Vmax is achieved. Higher the Km, lower the affinity of enzyme for substate and eventually high substrate concentration required for the reaction to occur.
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