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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]
On the other hand, the V max will decrease relative to an uninhibited enzyme. On a Lineweaver-Burk plot, the presence of a noncompetitive inhibitor is illustrated by a change in the y-intercept, defined as 1/V max. The x-intercept, defined as −1/K M, will remain the same. In competitive inhibition, the inhibitor will bind to an enzyme at the ...
The Monod equation is a mathematical model for the growth of microorganisms. It is named for Jacques Monod (1910–1976, a French biochemist, Nobel Prize in Physiology or Medicine in 1965), who proposed using an equation of this form to relate microbial growth rates in an aqueous environment to the concentration of a limiting nutrient.
At 298 K, a reaction with ΔG ‡ = 23 kcal/mol has a rate constant of k ≈ 8.4 × 10 −5 s −1 and a half life of t 1/2 ≈ 2.3 hours, figures that are often rounded to k ~ 10 −4 s −1 and t 1/2 ~ 2 h. Thus, a free energy of activation of this magnitude corresponds to a typical reaction that proceeds to completion overnight at room ...
In game theory, the one-shot deviation principle (also known as the single-deviation property [1]) is a principle used to determine whether a strategy in a sequential game constitutes a subgame perfect equilibrium [2]. An SPE is a Nash equilibrium where no player has an incentive to deviate in any subgame.
The function f(x, y) = x 2 − y 2 is concave-convex.. Von Neumann's minimax theorem can be generalized to domains that are compact and convex, and to functions that are concave in their first argument and convex in their second argument (known as concave-convex functions).
Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product.
Hanes noted that the use of linear regression to determine kinetic parameters from this type of linear transformation generates the best fit between observed and calculated values of /, rather than . [4]: 1415 Starting from the Michaelis–Menten equation: