No, trimethoprim is not an enzyme inducer. It is an antibiotic that works by interfering with the production of tetrahydrofolic acid, which is essential for the growth of bacteria.
The binding of a molecule at the allosteric site can induce a conformational change in the enzyme, affecting the active site's shape and activity. This can either increase or decrease the enzyme's affinity for its substrate, leading to changes in the enzyme's catalytic efficiency.
Factors that could impact the function of an enzyme include temperature, pH levels, substrate concentration, enzyme concentration, presence of inhibitors or activators, and cofactors or coenzymes. These factors can alter the enzyme's structure, affecting its ability to bind to substrates and catalyze reactions efficiently.
pH can impact crystal growth by affecting the solubility of the crystal components in the solution. Changing the pH can alter the balance between dissolved and undissolved components, potentially promoting or inhibiting crystal formation. Additionally, pH can influence the surface charge of the crystal, affecting the rate of crystal growth.
When the pH is above or below the optimum range for peroxidase, the enzyme's activity decreases. This is because the active site of the enzyme is influenced by the pH, affecting its ability to bind to the substrate. Consequently, the enzyme's catalytic function is compromised, leading to reduced efficiency in catalyzing the reaction.
you can say enzyme reaction depends on ph, temp
Concentration ( enzyme to substrate ), temperature and pH.
polymerase
Lysoszyme
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Enzyme activity is highly dependent on pH. Each enzyme has an optimal pH range where it functions most effectively. Deviation from this optimal pH can cause denaturation or inhibition of the enzyme, ultimately affecting its activity. pH can influence the ionization state of amino acid side chains in the enzyme's active site, affecting substrate binding and catalysis.
Predation
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No, trimethoprim is not an enzyme inducer. It is an antibiotic that works by interfering with the production of tetrahydrofolic acid, which is essential for the growth of bacteria.
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Non-competitive inhibition. This type of inhibition occurs when the inhibitor binds to a site on the enzyme that is different from the active site, causing a conformational change in the enzyme and affecting its ability to bind substrate. The inhibitor can bind to both the free enzyme and the enzyme-substrate complex with equal affinity.
Telomerase is responsible for indefinite growth of human cancer cells.