Very high activation energy is needed in enzymelss reactions
The enzyme activity curve shows that as enzyme concentration increases, the reaction rate also increases. However, there is a point where adding more enzyme does not further increase the reaction rate, indicating that there is a limit to the effect of enzyme concentration on reaction rate.
Without knowing the enzyme you are interested in, it is hard to give an exact answer. It all depends on the amount of the substrate, temperature, the resultant product, whether either is involved in a chain reaction or a simple reaction and if there is a co-enzyme involved. See the link below for more information on the reaction:
An enzyme is a protein that catalyzes a specific chemical reaction. The active site is a region on the enzyme where the substrate binds and the catalytic reaction takes place. The active site is crucial for the enzyme to function properly and interact with its substrate.
The enzyme graph shows that the reaction rate of the catalyzed reaction is faster compared to the uncatalyzed reaction. This indicates that the enzyme is effectively speeding up the reaction process.
Tobin can conclude that the reaction rate is directly proportional to the enzyme concentration when excess substrate is present. This is because at higher enzyme concentrations, all substrate molecules are already bound to enzyme active sites, leading to a maximal reaction rate even with excess substrate.
A nonenzymatic reaction doesn't use an enzyme.
There is no difference. An enzyme is a natural catalyst. Catalysts speed up the rate of reaction without being used up itself.
co factor helps the factor in reaction and co enzyme helps the enzyme only
enzyme is a kind of protein that catalyzes specific reactions & abzymes are antibodies that target the transition state of an expected reaction.
The change in ∆G would not be affected by doubling the amount of enzyme in the reaction. The ∆G value of a reaction represents the intrinsic energy difference between the products and the reactants, and it is not altered by enzyme concentration.
Enzymes do not affect the equilibrium point of a reaction they catalyze. Instead, enzymes increase the rate of reaction by lowering the activation energy barrier. The equilibrium point of a reaction is determined by the free energy difference between products and reactants at equilibrium, which remains unchanged in the presence of an enzyme.
what coenzyme reduce without altering rate of reaction
ENzyme
The presence of an enzyme lowers the activation energy required for the reaction to occur, as indicated by the red line being positioned lower than the black line. This results in an increased rate of reaction, allowing the reaction to proceed more quickly. Enzymes facilitate the conversion of substrates to products more efficiently without being consumed in the process. Overall, the use of an enzyme enhances the reaction's speed while maintaining the same overall thermodynamic outcome.
The enzyme activity curve shows that as enzyme concentration increases, the reaction rate also increases. However, there is a point where adding more enzyme does not further increase the reaction rate, indicating that there is a limit to the effect of enzyme concentration on reaction rate.
ENZYME
In an enzyme lab, the control is a sample that does not contain the enzyme being tested or is exposed to conditions that do not trigger the enzymatic reaction. This control helps establish a baseline for comparison, allowing researchers to determine the effect of the enzyme under various experimental conditions. By measuring the difference in reaction rates or product formation between the experimental samples and the control, scientists can assess the enzyme's activity and effectiveness.