Search results
Results from the WOW.Com Content Network
in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...
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).
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.
The chemical mechanism can also be elucidated by examining the kinetics and isotope effects under different pH conditions, [47] by altering the metal ions or other bound cofactors, [48] by site-directed mutagenesis of conserved amino acid residues, or by studying the behaviour of the enzyme in the presence of analogues of the substrate(s).
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]
Any metabolic or chemical messenger system can potentially be affected by this principle, but several classes of competitive inhibition are especially important in biochemistry and medicine, including the competitive form of enzyme inhibition, the competitive form of receptor antagonism, the competitive form of antimetabolite activity, and the ...
They are classified according to the effect of the inhibitor on the V max (maximum reaction rate catalysed by the enzyme) and K m (the concentration of substrate resulting in half maximal enzyme activity) as the concentration of the enzyme's substrate is varied. [15] [16]
This enzymatic regulation may be indirect, in the case of an enzyme being regulated by some cell signalling mechanism (like phosphorylation), or it may be direct, as in the case of allosteric regulation, where metabolites from a different portion of a metabolic network bind directly to and affect the catalytic function of other enzymes in order ...