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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 second assumption is that the total enzyme concentration does not change over time, thus [] = [] + [] =!. The Michaelis constant K M is experimentally defined as the concentration at which the rate of the enzyme reaction is half V max , which can be verified by substituting [S] = K M into the Michaelis–Menten equation and can also be seen ...
Michaelis–Menten kinetics have also been applied to a variety of topics outside of biochemical reactions, [14] including alveolar clearance of dusts, [19] the richness of species pools, [20] clearance of blood alcohol, [21] the photosynthesis-irradiance relationship, and bacterial phage infection. [22]
The rate of a reaction is the concentration of substrate disappearing (or product produced) per unit time (mol L −1 s −1).. The % purity is 100% × (specific activity of enzyme sample / specific activity of pure enzyme).
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 ability of glucose-6-phosphate to bind at different places at the same time makes it a non-competitive inhibitor. [ 7 ] The most common mechanism of non-competitive inhibition involves reversible binding of the inhibitor to an allosteric site , but it is possible for the inhibitor to operate via other means including direct binding to the ...
a possible mechanism of non-competitive inhibition, a kind of mixed inhibition.. Mixed inhibition is a type of enzyme inhibition in which the inhibitor may bind to the enzyme whether or not the enzyme has already bound the substrate but has a greater affinity for one state or the other. [1]
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