Which of the following is true for enzyme catalyzed reactions ?
Km is affinity constant
In Michaelis–Menten kinetics, v = Vmax[S] / (Km + [S]). Km is the substrate concentration at which the velocity is half of Vmax, and it has units of concentration.
When the breakdown of the enzyme–substrate complex to product is slow compared with its dissociation, Km approximates the dissociation constant of the ES complex. It is therefore used as a measure of the affinity of an enzyme for its substrate (a low Km means high affinity), which is why it is described as an affinity constant.
Vmax is the rate when all enzyme molecules are saturated with substrate; at substrate concentrations far above Km the measured velocity is practically equal to Vmax, so it is attainable in practice even though the hyperbola approaches it asymptotically.
The relations Km = ½Vmax and Km = Vmax are meaningless because Km is a concentration while Vmax is a rate; the correct relation is that v = ½Vmax when [S] = Km.
Hence, Km is affinity constant.
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