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  2. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1] For enzymes with a single active site, k cat is referred to as the catalytic constant. [2]

  3. Dissociation rate - Wikipedia

    en.wikipedia.org/wiki/Dissociation_rate

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

  4. Diffusion-limited enzyme - Wikipedia

    en.wikipedia.org/wiki/Diffusion-limited_enzyme

    Kinetically perfect enzymes have a specificity constant, k cat /K m, on the order of 10 8 to 10 9 M −1 s −1. The rate of the enzyme-catalysed reaction is limited by diffusion and so the enzyme 'processes' the substrate well before it encounters another molecule. [1]

  5. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The substrate concentration midway between these two limiting cases is denoted by K M. Thus, K M is the substrate concentration at which the reaction velocity is half of the maximum velocity. [2] The two important properties of enzyme kinetics are how easily the enzyme can be saturated with a substrate, and the maximum rate it can achieve.

  6. Kinetics - Wikipedia

    en.wikipedia.org/wiki/Kinetics

    Kinetics (physics), the study of motion and its causes Rigid body kinetics, the study of the motion of rigid bodies; Chemical kinetics, the study of chemical reaction rates Enzyme kinetics, the study of biochemical reaction rates catalysed by an enzyme Michaelis–Menten kinetics, the widely accepted general model of enzyme kinetics

  7. Binding constant - Wikipedia

    en.wikipedia.org/wiki/Binding_constant

    The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL

  8. Kinesiology - Wikipedia

    en.wikipedia.org/wiki/Kinesiology

    A series of images that represent research (left) and practice (right) in the field of academic kinesiology. Kinesiology (from Ancient Greek κίνησις (kínēsis) 'movement' and -λογία-logía 'study of') is the scientific study of human body movement.

  9. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    In biochemistry, a kinase (/ ˈ k aɪ n eɪ s, ˈ k ɪ n eɪ s,-eɪ z /) [2] is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule.