Dissociation rate

The dissociation rate in chemistry, biochemistry, and pharmacology is the rate or speed at which a ligand dissociates from a protein, for instance, a receptor.[1] It is an important factor in the binding affinity and intrinsic activity (efficacy) of a ligand at a receptor.[1] The dissociation rate for a particular substrate can be applied to enzyme kinetics, including the Michaelis-Menten model.[2] Substrate dissociation rate contributes to how large or small the enzyme velocity will be.[2] In the Michaelis-Menten model, the enzyme binds to the substrate yielding an enzyme substrate complex, which can either go backwards by dissociating or go forward by forming a product.[3] The dissociation rate constant is defined using Koff.[2]


References
  1. Wanner K, Höfner G (27 June 2007). Mass Spectrometry in Medicinal Chemistry: Applications in Drug Discovery. John Wiley & Sons. pp. 142–156. ISBN 978-3-527-61091-4.
  2. Berezhkovskii AM, Szabo A, Rotbart T, Urbakh M, Kolomeisky AB (April 2017). "Dependence of the Enzymatic Velocity on the Substrate Dissociation Rate". The Journal of Physical Chemistry B. 121 (15): 3437–3442. doi:10.1021/acs.jpcb.6b09055. PMC 5577799. PMID 28423908.
  3. Berezhkovskii AM, Szabo A, Rotbart T, Urbakh M, Kolomeisky AB (April 2017). "Dependence of the Enzymatic Velocity on the Substrate Dissociation Rate". The Journal of Physical Chemistry B. 121 (15): 3437–3442. doi:10.1021/acs.jpcb.6b09055. PMC 5577799. PMID 28423908.
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