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In chemistry, the term "turnover number" has two distinct meanings.. 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]
In the field of biochemistry, the specificity constant (also called kinetic efficiency or /), is a measure of how efficiently an enzyme converts substrates into products.A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.e., substrate specificity).
The Lineweaver–Burk plot derives from a transformation of the Michaelis–Menten equation, v = V a K m + a {\displaystyle v={\frac {Va}{K_{\mathrm {m} }+a}}} in which the rate v {\displaystyle v} is a function of the substrate concentration a {\displaystyle a} and two parameters V {\displaystyle V} , the limiting rate , and K m {\displaystyle ...
Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics. The rate of reaction of many chemical reactions shows a linear response as function of the concentration of substrate molecules.
Like other techniques that linearize the Michaelis–Menten equation, the Hanes–Woolf plot was used historically for rapid determination of the kinetic parameters , and /, but it has been largely superseded by nonlinear regression methods that are significantly more accurate and no longer computationally inaccessible. It remains useful ...
The katal (symbol: kat) is that catalytic activity that will raise the rate of conversion by one mole per second in a specified assay system. [1] It is a unit of the International System of Units (SI) [1] used for quantifying the catalytic activity of enzymes (that is, measuring the enzymatic activity level in enzyme catalysis) and other catalysts.
Determining the parameters of the Michaelis–Menten equation typically involves running a series of enzyme assays at varying substrate concentrations , and measuring the initial reaction rates , i.e. the reaction rates are measured after a time period short enough for it to be assumed that the enzyme-substrate complex has formed, but that the ...
In graph theory, Graph equations are equations in which the unknowns are graphs. One of the central questions of graph theory concerns the notion of isomorphism. We ask: When are two graphs the same? (i.e., graph isomorphism) The graphs in question may be expressed differently in terms of graph equations. [1]