Dissociation rate

The dissociation rate in

The Michaelis-Menten constant is denoted by K_m and is represented by the equation K_m= (K_off + K_cat)/ K_on^[definition needed]. The rates that the enzyme binds and dissociates from the substrate are represented by K_on and K_off respectively. K_m is also defined as the substrate concentration at which enzymatic velocity reaches half of its maximal rate.^[3] The tighter a ligand binds to a substrate, the lower the dissociation rate will be. K_m and K_off are proportional, thus at higher levels of dissociation, the Michaelis-Menten constant will be larger.^[4]

Direct measurements using electrospray ionization mass spectrometry (ESI-MS) have quantified dissociation rate constants for high-affinity ligand-protein interactions, such as the biotin-streptavidin system, offering a deeper understanding of enzyme-substrate dynamics.^[5] Recent computational studies have provided insights into the diffusional processes that influence the dissociation rates of bio-molecular complexes, highlighting the importance of molecular movement and binding specificity in these interactions, the importance is considering both the physical movement of molecules and their binding specificities when analyzing dissociation rates.^[6]

References

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