Alkaline concentratipn 8. Effect of Co-enzymes concentration Co-enzymes concentration has the same effect and gives the same curve of substrate concentration on enzymatic activity, as NAD. http://rectoria.unal.edu.co/uploads/tx_felogin/children-at-home-and-abroad/pope-gregory-vii-and-king-henry-iv.php of physical agents Red and blue lights increase enzyme activity. Heating, shaking stirring inhibit enzyme activity by denaturation. Ultraviolet rays and infrared rays inhibit enzyme activity. Effect of enzymatic activators Activators increase the rate of enzyme -catalyzed reactions. The velocity of the reaction depends on activator concentration.
The Effect Of Temperature On Enzyme Activity
Some enzymes are activated by different ways: Removal of inhibitory peptide converts inactive forms of the enzyme zymogen or proenzyme to the active forms. The inhibitory peptide usually masks the catalytic site. Some enzymes require minerals, they are called metal activated enzymes e. Allosteric activators.
Allosteric modifiers The binding of the allosteric activator produces conformational changes in the protein structure of the enzyme resulting in increased velocity of the reaction e. AMP is an allosteric activator of phosphofructokinase enzyme. Covalent modification: Many enzymes are activated by phosphorylation and inactivated by dephosphorylation and vice versa. This means that the enzyme is present in two interconvertible forms phosphorylated and dephosphorylated.
The phosphate groups are usually attached to the hydroxyl group of amino acid residues mainly serine emzyme tyrosine in the polypeptide chain of the enzyme. A good example is the activation of glycogen phosphorylase and hormone-sensitive lipase by phosphorylation while the activation of glycogen synthase is by dephosphorylation. Effect of enzymatic inhibitors Inhibitors are substances that combine with the effect of enzyme concentration competitively or non-competitively leading to the decreased catalytic activity of the enzyme. Types: 1 Competitive substrate analogue inhibition The inhibitor I combines with the enzyme E at the catalytic site.
Effect Of Temperature On Enzyme Activity
The chemical structure of the inhibitor closely resembles that of the substrate. When both the substrate and the inhibitor are present, they compete for the same binding site catalytic site on the enzyme surface. In this type of inhibition, the Vmax of the enzyme is not decreased, but the apparent Km is increased i. This type of inhibition is reversible and the inhibition is removal by increasing article source substrate concentration. Example: Malonic acid is similar in structure to succinic acid so, it competes with is at the catalytic site of succinic effect of enzyme concentration dehydrogenase leading to its inhibition which can be reversed by increasing succinic acid concentration.]