### Understanding Competitive Inhibition**A competitive inhibitor** is a molecule that affects enzyme activity in biochemical reactions. Here are some key points about how competitive inhibitors function:- **Has little effect on the reaction at very high substrate concentration**: Competitive inhibitors are less effective when there is a high concentration of substrate. The substrate can outcompete the inhibitor for the active site of the enzyme, reducing the inhibitor's effect.- **Binds to the active site of an enzyme**: The competitive inhibitor mimics the substrate structure and binds to the enzyme's active site. This prevents the actual substrate from binding, thereby reducing the reaction rate under normal conditions.- **Slows the reaction down at low substrate concentrations**: At low substrate concentrations, competitive inhibitors significantly slow down the reaction by effectively blocking the active site and preventing substrate binding.Understanding these dynamics is crucial for comprehending how enzymes are regulated in biological processes.

Answered: pinds to the active site of an enzyme…

Science

Chemistry

pinds to the active site of an enzyme clows the reaction down at low substrat

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Related questions

Q: A.) A B.) B C.) C

Q: Reaction rate data of an enzyme, E, and a substrate, S, with increasing inhibitor concentrations are…

Q: Calculate the standard error of regression (SER) for the Lineweaver-Burk slope and the Eadie-Hofstee…

A: NOTE : FOR LINEWEAVER-BURK PLOT: THE SLOPE OF 1/V0 VS 1/[S] IS EQUAL TO FOR EADIE HOPSTEE PLOT:

Q: 1. Determining Km and Vmax. You have recently discovered a new enzyme homeworkase which destroys…

A: The rate equation for Michaelis Menten equation is given as, R= K2SES +KM where,S = substrate…

Q: sac ve inhihi. following graph shows the activity versus pH curves for pepsin, sucrase, and trypsin.…

A: Optimum pH is the pH at which the enzyme has maximum activity. Optimum rate is the maximum rate that…

Q: For the reaction A-->B, when [A] = Km and the enzyme concentration is 3 x 10-8 M (3 x 10-2μM), the…

Q: What mutant of Dihydroorotase affected the most it's turnover rate? Estimate its impact on the…

A: The objective of this question is to show the mutants is one that has a significant effect on…

Q: 4. The following rate constants have been determined for a Michaelis –Menen enzyme: ki = 2.5 x 10$…

Q: The decomposition the way it and the following uald were obtained: 2 H₂O2(aq) 40 °C Time (s) [H₂0₂]…

Q: One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover…

A: First convert the given time in second and use that time to calculate molecules of ribonuclease act…

Q: A certain reaction is catalyzed by an enzyme at body temperature. When the substrate's concentration…

Q: The figure below shows the dependence of the enzyme's rate, v (in uM/min), as a function of…

A: Lineweaver–Burk plot gives the value of Vmax for the enzyme.

Q: An enzyme catalyzed the reaction: S -> P has a AG°' value of +4.8 kJ/mol. If you start with a…

A: The given catalyzed reaction is:

Q: The equilibrium constant for the binding of a substrate to the active site of an enzyme was measured…

Q: Which one of the following is true regarding our coverage of enzyme kinetics? Increasing the…

A: Fourth option is correct.

Q: 29.Which amino acid is ideal for the transfer of protons within the catalytic site of enzymes due to…

A: Histidine is an amino acid that possesses a unique property in its side chain. At biological pH,…

Q: The following 5-step mechanism is proposed for the folding pathway of a protein: 1. Unfolded Protein…

A: While the rate law’s prediction for any certain reaction mechanism, the intermediate must be…

Q: 7. A group of Colby students discovered a hydrolase that cleaves cellulose. After purifying the…

Q: 4. Suppose the data shown below are obtained for an enzyme catalyzed reaction. [S] (MM) v…

A: The equation is in the straight line, y=mx+b, form. So, we need to plot 1/V on y-axis and 1/[S] on…

Q: What is the activation energy of a reaction? Select the single best answer. The energy required for…

A: The progress of a reaction can be represented by the reaction coordinate diagram. In a reaction…

Q: The following results were obtained for an enzyme-catalyzed reaction Substrate concentration (mmol…

A: The objective of this question is to calculate the Michaelis-Menten constant (Km) and the maximum…

Q: If %T for sample A is 0.005%T and for sample B it is 25%T at 10 minutes after adding enzyme, which…

A: In the given question we have to choose the correct sample which shows the enzyme activity.…

Q: hy does adding the reaction mix to the “stop” tubes immediately stop the enzymic reaction?

A: Raising temperature generally speeds up a reaction, and lowering temperature slows down a reaction.…

Q: Number 4 on the Reaction Energy diagram below represents Ep (kJ) reactants Reaction Coordinate…

A: When the reactant molecules convert into products, they require the minimum amount of excess energy.…

Q: Use the data below to determine the Michaelis-Menton constant [in mM] of a certain enzyme-catalyzed…

A: Given that, v1 = 0.152 mM/s at [S1] = 0.334 mM, And v2 = 0.176 mM/s at [S2] = 0.450 mM. We have to…

Q: 6.) Vmax represents the rate of reaction for an enzyme-substrate pairing under what conditions? B)…

A: Value of Michaelis constant (km) tells about the affinity of enzyme to the substrate.

Q: What parameters associated with enzyme activity are related to the Arrhenius equation? How can those…

A: EXPLANATION: ⦁ The dependence of the rate constant in a chemical reaction is given in Arrehenius…

Q: Juan performed the same chemical reaction twice. His data from the first at- tempt is indicated by…

A: From the above diagram it is clear that overall energy released during the reaction for both…

Q: Consider the following enzyme-catalyzed reaction: S - P Which of the following statements are…

A: The Enzyme catalyzed reaction proceeds as: E+S ⇋k-1k1 ESES →k2 P+E The rate of this reaction is…

Q: 8. Data on the speeds of a Michaelis-Menten enzyme reaction v (in micromolar/minute) as a function…

Q: Although there are accurate graphical methods available for determining Vmax and Km of an…

A: Approach to solving the question: Detailed explanation: Vmax and Km for the enzyme-catalyzed…

Q: a. Graph and explain the relationship between the reaction rate and the enzyme concentration. b.…

A: In biology, chemical reactions are often supported by enzymes, biological molecules made of proteins…

Q: Practice 14: The following is a schematic of an active site in an enzyme. Considering the shape and…

A: The objective of this question is to explain the enzymes which are proteins that catalyze chemical…

Question

### Understanding Competitive Inhibition

**A competitive inhibitor** is a molecule that affects enzyme activity in biochemical reactions. Here are some key points about how competitive inhibitors function:

- **Has little effect on the reaction at very high substrate concentration**: Competitive inhibitors are less effective when there is a high concentration of substrate. The substrate can outcompete the inhibitor for the active site of the enzyme, reducing the inhibitor's effect.

- **Binds to the active site of an enzyme**: The competitive inhibitor mimics the substrate structure and binds to the enzyme's active site. This prevents the actual substrate from binding, thereby reducing the reaction rate under normal conditions.

- **Slows the reaction down at low substrate concentrations**: At low substrate concentrations, competitive inhibitors significantly slow down the reaction by effectively blocking the active site and preventing substrate binding.

Understanding these dynamics is crucial for comprehending how enzymes are regulated in biological processes.

Expert Solution

Step 1

A competitive inhibitor binds to the active site of an enzyme.

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Similar questions

What chemical reaction is being catalyzed in this experiment? Label the substrate(s), enzyme and product(s). Based on the information in the data table and your graph, is there an optimum temperature for catalase that makes it the most productive in terms of reaction rate? If so, what is the temperature? 3. At what temperature, does the rate of the reaction decrease? Explain why.
Below which is false about the Michaelis constant Km in Michaelis-Menten kinetics? k₂ k₁ E+SESE + P k₁ k₂ A higher K indicates a higher affinity between the substrate and the enzyme. Km is effectively equal to the Dissociation Constant (k_₁/k₁) for ES. When [Substrate] = Km, Vo = 1/2 V max When [Substrate] = Km [ES] = [Efree] = [Etotal]
Please provide only typed answer solution no handwritten solution needed allowed
The enzyme examase catalyses the following reaction, A - B where A is the reactant and B is the product A595 measurements were used to determine the catalytic activity of examase by measuring the rate at which B is produced. From this, the activity of the enzyme was determined to be 42 µmol/mL per minute. A standard albumin solution (concentration = 10 mg/mL) was used to prepare a standard curve of Abs595 vs amount of protein in mg. The protein assay was also performed using 100 uL of a 1 in 10 dilution of the original examase sample. For the absorbance measurements, it was determined that the sample used in the A595 measurement contains 1.2 mg of examase. Which of the following statements correctly gives the specific activity of examase? 1.0.35 U/mg O 2.0.035 U/mg 3. 5040 U/mg O 4.35 U/mg O 5.3.5 U/mg
help please answer in text form with proper workings and explanation for each and every part and steps with concept and introduction no AI no copy paste remember answer must be in proper format with all working
Examine this depiction of the initial steps of catalysis for a proteolytic enzyme. Oxyanion hole 93 with In 1-2 sentences, describe the role being played by the amino acid hydroxyl side chain in the step labeled 2. In 1-2 sentences, describe the role of the oxyanion hole. In 1-2 sentences, describe the role of the His is the step labeled 3.
What solution asap....