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Is a ribozymes a horomones inhibitors cofactora or enzymes?
They're catalysts like enzimes, but they're not actually enzymes, which are proteic.
Why negative catalyst called inhibitors?
Negative catalysts (inhibitors) are those substances (or factors) which slow down the chemical reactions by decreasing the required activation energy for the reaction, for example the decomposition of Hydrogen peroxide may be slow down by adding a small amount of Glycerin in it.
What are four ways that chemists can control chemical reactions?
increase in surface area, increase in temperature, increase the concentration of the reactants, and the presence of catalysts or inhibitors.
What are four ways that chemists control the rates of chemical reactions?
Increase in Surface area,Increase in temperature,Increase in concentration,and the presence of catalysts or inhibitors.
What are the activity levels of compounds are affected by?
The activity levels of compounds can be affected by factors such as temperature, concentration, pH, solvent polarity, and the presence of catalysts or inhibitors. These factors can influence the rate of reactions, solubility, and stability of compounds.
How do competitive and noncompetitive inhibitors differ in their mechanisms of action and impact on enzyme activity?
Competitive inhibitors compete with the substrate for the enzyme's active site, while noncompetitive inhibitors bind to a different site on the enzyme. Competitive inhibitors can be overcome by increasing substrate concentration, while noncompetitive inhibitors cannot. Both types of inhibitors reduce enzyme activity, but competitive inhibitors specifically affect the binding of the substrate, while noncompetitive inhibitors can alter the enzyme's shape or function.
Competitive and noncompetitive enzyme inhibitors differ with respect to?
Competitive inhibitors bind to the active site of the enzyme, competing with the substrate, while noncompetitive inhibitors bind to a site other than the active site, changing the enzyme's shape and preventing substrate binding. Competitive inhibitors can be overcome by increasing substrate concentration, while noncompetitive inhibitors cannot.
What are 3 characteristics of enzymes?
Enzymes are biological catalysts that speed up chemical reactions in living organisms. Enzymes are specific in their action, meaning they catalyze specific reactions and substrates. Enzymes can be regulated by factors such as temperature, pH, and inhibitors.
Compare and contrast a catalyst and an inhibitor?
Catalysts increase the rate of reaction while Inhibitors decrease it. They both affect the rate of reaction, hence giving us more control over our reaction.
One way in which inorganic catalysts and enzymes differ is?
Inorganic catalysts are typically synthetic molecules while enzymes are biological molecules. Enzymes are highly specific to their substrates due to their complex three-dimensional structures, whereas inorganic catalysts are less specific and can catalyze a wider range of reactions. Enzymes are usually more efficient in catalyzing reactions compared to inorganic catalysts.
What are catalysts that slow down a reaction?
The catalysts can be used to increase or decrease the speed of a chemical reaction. The catalysts which reduce the speed of a reaction are called negative catalysts. They decrease the speed of the reaction by increasing the activation energy of the reaction.
How do noncompetitive and allosteric inhibitors differ in their mechanisms of action on enzymes?
Noncompetitive inhibitors bind to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and preventing substrate binding. Allosteric inhibitors bind to a different site on the enzyme, causing a conformational change that affects the active site's ability to bind substrate.
