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  2. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    The model is used in a variety of biochemical situations other than enzyme-substrate interaction, including antigen–antibody binding, DNA–DNA hybridization, and protein–protein interaction. [ 17 ] [ 18 ] It can be used to characterize a generic biochemical reaction, in the same way that the Langmuir equation can be used to model generic ...

  3. Reversible Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Reversible_Michaelis...

    When used to model enzyme rates in vivo , for example, to model a metabolic pathway, this representation is inadequate because under these conditions product is present. As a result, when building computer models of metabolism [ 1 ] or other enzymatic processes, it is better to use the reversible form of the Michaelis–Menten equation.

  4. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The favoured model for the enzyme–substrate interaction is the induced fit model. [53] This model proposes that the initial interaction between enzyme and substrate is relatively weak, but that these weak interactions rapidly induce conformational changes in the enzyme that strengthen binding.

  5. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    The Michaelis–Menten Model can be an invaluable tool to understanding enzyme kinetics. According to this model, a plot of the reaction velocity (V 0 ) associated with the concentration [S] of the substrate can then be used to determine values such as V max , initial velocity, and K m (V max /2 or affinity of enzyme to substrate complex).

  6. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    The classic model for the enzyme-substrate interaction is the induced fit model. [3] This model proposes that the initial interaction between enzyme and substrate is relatively weak, but that these weak interactions rapidly induce conformational changes in the enzyme that strengthen binding.

  7. Dissociation rate - Wikipedia

    en.wikipedia.org/wiki/Dissociation_rate

    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. [2] The dissociation rate constant is defined using K off. [2]

  8. Metabolic network modelling - Wikipedia

    en.wikipedia.org/wiki/Metabolic_network_modelling

    Enzymes and metabolites are the red dots and interactions between them are the lines. Metabolic network model for Escherichia coli Metabolic network modelling , also known as metabolic network reconstruction or metabolic pathway analysis , allows for an in-depth insight into the molecular mechanisms of a particular organism.

  9. Enzyme induction and inhibition - Wikipedia

    en.wikipedia.org/wiki/Enzyme_induction_and...

    Enzyme induction is a process in which a molecule (e.g. a drug) induces (i.e. initiates or enhances) the expression of an enzyme. Enzyme inhibition can refer to the inhibition of the expression of the enzyme by another molecule; interference at the enzyme-level, basically with how the enzyme works.