K m is similar, but not exactly equal to, a dissociation constant (K d) for the ES complex; If k-1 >> k 2, then K m » K d; Due to this similarity to the expression for K d, a low value of K m is often interpreted as a high affinity of the enzyme for the substrate, and a large value for K m is often interpreted as a weak affinity of the enzyme for the substrate Michaelis constant (K m). All these questions can be answered in this series of short and handy videos listed below, check back regularly since we are always updating this page. The K m is an apparent dissociation constant of all enzyme-bound species. Kinetics of Calcium and Magnesium Binding. What is the dissociation constant KD? The dissociation constant is the ratio of the off rate to the on rate: Kd (M) = koff (s −1 )/ kon (M −1 s −1 ). The rate limiting dehydration of Ca ( H 2 O) 7 2 + is fast, ~10 8.0 s −1; while that of Mg ( H 2 O) 6 2 + is slow, ~10 4.6 s −1. In its reciprocal form (1/ K m), K m can be regarded as the binding affinity of an enzyme for its substrate. Biotin and avidin bind with a dissociation constant of roughly 10 −15 M = 1 fM = 0.000001 nM. Ribonuclease inhibitor proteins may also bind to ribonuclease with a similar 10 −15 M affinity. The lower the constant, the higher the affinity. ii. In the Michaelis-Menten mechanism, K m is equal to the substrate constant K s (= k – 1 /k 1). And where can I find it on the binding affinity curve? How do I calculate KD? The dissociation constant for a particular ligand-protein interaction can change significantly with solution conditions (e.g., temperature, pH and salt concentration).

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