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Most enzymes are sensitive to pH and have specific ranges of activity. All have an optimum pH. The pH can stop enzyme activity by denaturating (altering) the three-dimensional shape of the enzyme by breaking ionic, and hydrogen bonds. Most enzymes function between a pH of 6 and 8; however pepsin in the stomach works best at a pH of 2 and ...
Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier (inhibitor or activator) might affect the rate. An enzyme (E) is a protein molecule that serves as a biological catalyst to facilitate and accelerate a chemical ...
The cascade effect of phosphorylation eventually causes instability and allows enzymes to open the carbon bonds in glucose. Phosphorylation functions is an extremely vital component of glycolysis, as it helps in transport, control, and efficiency.
Intracellular pH (pH i) is the measure of the acidity or basicity (i.e., pH) of intracellular fluid. The pH i plays a critical role in membrane transport and other intracellular processes. In an environment with the improper pH i , biological cells may have compromised function.
Because a phosphatase enzyme catalyzes the hydrolysis of its substrate, it is a subcategory of hydrolases. [1] Phosphatase enzymes are essential to many biological functions, because phosphorylation (e.g. by protein kinases) and dephosphorylation (by phosphatases) serve diverse roles in cellular regulation and signaling. [2]
Sodium periodate oxidizes the sialic acids on glycoproteins to aldehydes to form these stable linkages at pH 4–6. Polyclonal antibodies are heavily glycosylated, and because glycosylation does not interfere with the antibody activity, biotinylating the glycosyl groups is an ideal strategy to generate biotinylated antibodies.
Kinetic studies show that malate dehydrogenase enzymatic activity is ordered. The cofactor NAD + /NADH is bound to the enzyme before the substrate. [15] The Km value for malate, i.e., the concentration at which the enzyme activity is half-maximal, is 2 mM. The Kcat value is 259.2 s −1. [16]
Triose phosphate isomerase is a highly efficient enzyme, performing the reaction billions of times faster than it would occur naturally in solution. The reaction is so efficient that it is said to be catalytically perfect: It is limited only by the rate the substrate can diffuse into and out of the enzyme's active site. [2] [3]