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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]
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.
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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).
Volumetric flow rate is defined by the limit [3] = ˙ = =, that is, the flow of volume of fluid V through a surface per unit time t.. Since this is only the time derivative of volume, a scalar quantity, the volumetric flow rate is also a scalar quantity.
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An anhydrase is defined as an enzyme that catalyzes the removal of a water molecule from a compound, and so it is this "reverse" reaction that gives carbonic anhydrase its name, because it removes a water molecule from carbonic acid. In the lungs carbonic anhydrase converts bicarbonate to carbon dioxide, suited for exhalation.
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.