I’m reviewing Enzyme Inhibition and am having issues wrapping my head around non-competitive and uncompetitive inhibition (and their consequent effect on Vmax / Km.)

Q: What are the factors to be considered in designing an enzyme kinetics experiment??

A: Enzymes are biological catalysts that increase the rates of reactions in cell but do not themselves…

Q: A researcher has measured the initial rate of an enzyme-catalyzed reaction as a function of…

A: Km and Vmax are important features of an enzyme thatvcan determine the efficiency of the enzyme.…

Q: Can you please help me answer the following question in three paragraphs and in your own words.…

A: Enzymes are substances that enhance the rate of chemical reaction and facilitate the formation of…

Q: f the new higher KM value is 0.1 mM resulting in the new plot red curve is due to presence of…

A: Km is Substrate concentration at half Vmax. It can be calculated from Michael's Menton plot or lb…

Q: Explain the various forms of enzyme inhibitions in detail, using appropriate examples. Please be…

A: Enzymes bind to substrate molecules through their active site and increase the rate of conversion…

Q: What do you mean by feedback inhibition or end-product inhibition ?

A: Feedback inhibition is a type of regulating activity, in which an enzyme is inhibited by their end…

Q: VO (mM/min), Minus Substrate, mM vO (mM/min), Plus Inhibitor Inhibitor 0.5 23.5 16.67 1 32.2 25.25…

A: The reciprocal of the given kinetic data is as follows: 1/[S] mM-1 1/V (min/mM) minus inhibitor…

Q: Compare the mechanisms of competitive and noncompetitive inhibition of enzymes.

A: The cell uses specific molecules for enzyme regulation in order to promote or inhibit specific…

Q: indicate how the observed Km of an enzyme would change in the presence of inhibitors having the…

A: The Km is known as Michaelis constant, it is the concentration of substrate at which reaction…

Q: What is the difference between the left and right? What type of inhibition is being shown? What are…

A: Note: Since you have posted multiple independent questions in the same request, we will solve the…

Q: [Substrate, uM] Vo with DEDS (µM/min) Vo without DEDS (µM/min) 3.333 0.774 1.196 4.000 0.877 1.316…

A: Given data of interest (X, Y) values where X denotes the substrate concentration in uM and Vo…

Q: A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown…

A: The rate of enzyme catalyzed reactions is directly proportional to the substrate concentration. But,…

Q: Define

A: Enzyme kinetic is a branch of Biochemistry. There are several factors that enzyme catalysis are…

Q: Briefly explain the Michaelis-Menten model of enzyme kinetics.

A: Enzymes are commonly composed of protein molecules that catalyze the biochemical reaction by…

Q: Compare the KM and Vmax of the enzyme in the absence and presence of inhibitors to determine what…

A: Inhibitors are the molecules which decrease the efficiency of enzyme activity.

Q: A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere…

A: Enzymes are biocatalyst that increases the rate of reaction. Enzyme inhibition can be of 5 types :-…

Q: A plot of 1/Vo versus 1/[S], called Lineweaver-Burk or double-reciprocal plot, is a useful tool for…

A: Lineweaver-Burk plot is also known as the double reciprocal plot. Plot between the reciprocal of…

Q: What is the biological purpose of enzyme regulation, i.e., why is it necessary to regulate enzyme…

A: Introduction: Enzymes are biological catalysts that are synthesized by the living cells of the body.…

Q: Define and contrast competitive and non-competitive inhibition.

A: The enzyme activity can be inhibited by the binding of small molecules or ions. The process by which…

Q: Essay: In your own words explain the following concept in not more than 5 sentences a. The lock and…

A: A. The lock and key model showing enzyme-substrate interaction. In which the substrate behave like…

Q: Since KM is an intrinsic property of an enzyme, its value does not depend on the enzyme…

A: Km is the Michaelis constant. It is defined as the substrate concentration at which half of the Vmax…

Q: (s) mM

A: Given graph is a double reciprocal plot or Lineweaver plot. The graph is plotted between reciprocal…

Q: In the induced-fit model of enzyme action, the active site on the enzyme provides an exact fit for…

A: Enzyme are substances that catalyze chemical reactions. They bind to reactant molecules, called…

Q: Given the active site diagram and reaction mechanism, indicate the mechanism of irreversible…

A: Irreversible inhibition is a process in which inhibitors bind covalently or non-covalently to a…

Q: You measure the initial rate of an enzyme reaction as a function of substrate concentration in the…

A: Enzyme kinetics follow Michealis Menton equation which is Vo = Vmax[S]/(Km + [S]). It can be…

Q: Given below are five Km values for the binding of substrates to a particular enzyme. Which substrate…

A: Those proteins or biological catalysts which help to speed up the chemical reaction are termed…

Q: An Eadie-Hofstee plot is shown below for the different types of enzyme inhibition. Match the line…

A: Eadie-Hofstee diagram also called as Woolf-Eadie-Augustinsson-Hofstee or Eadie-Augustinsson plot is…

Q: You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered…

A: Lineweaver-Burk plot, also known as double-reciprocal plot, is the graph plotted for Lineweaver-Burk…

Q: What are two major types of enzyme inhibitors? Give an example of each

A: Enzyme inhibitors can be defined as the substance or molecule which binds to the enzyme and inhibits…

Q: A noncompetitive inhibition is best overcome (or reversed) by: A. Increasing [enzyme] B. Increasing…

A: Competitive inhibition is the process in which a chemical substance inhibits the effect of another…

Q: Define the word "enzyme inhibition."

A: Enzymes are protein molecules that aid in the speeding up of chemical processes. Enzyme, in other…

Q: If 287.9 umol of enzyme X has a Vmax = 47.8 mmol/sec, what is the value of kcat sec-1? Please report…

A: Enzymes are biological catalysts that help in catalyzing or speeding up biological reactions by…

Q: A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown…

A: To determine the values of km and Vmax by lineae regression, we need to plot lb plot. LB plot can be…

Q: Please choose one of these answers A. An allosteric inhibitor appeared B. There was a dramatic…

A: Enzymes are the molecules which speed up the rate of biological reactions without being consumed in…

Q: What are the meanings and differences between Ki, Km, and IC50? Are there certain advantages or…

A: Enzymes are biocatalyst. They speed up the rate of biochemical reaction. Enzyme binds with substrate…

Q: Why might an enzyme’s substrate, transition state, and product all serve as starting points for the…

A: Enzymes are proteins, which acts as a catalyst and helps to convert substrate into the product,…

Q: What are the optimal conditions for an enzyme(full answer)?

A: Since you have asked multiple question, we will solve the first question for you. If you want any…

Q: The Michaelis-Menten constant Km is O a. Dependent on the enzyme concentration b. Numerically equals…

A: Ans- The Michalis-Menton constant Km is the concentration of the substrate at which an enzyme…

Q: Write the difference between compititive and non compititive enzyme inhibitors.

A: Enzyme inhibitors binds with the active sites of enzymes and reduces the compatibility of substrate…

Q: Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the ab- sence…

A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…

Q: Explain why it is usually easier to calculate an enzyme’s reaction velocity from the rate of…

A: Enzymes are proteins that alter the rate of the reaction, that is alter the rate in which the…

Q: The initial rate for an enzyme-catalyzed reaction has been determined at several substrate…

A: The substrate concentration and velocity is put into the following chart:

Q: List down the properties of an ideal carrier matrix for enzyme immobilization.

A: Enzymes can be used as catalytic agents in medical and industrial applications. Such enzymes are…

Q: The factors that denature enzyme activity are temperature, pH, salinity, alcohol and surface area.

A: Enzyme are biocatalyst and protenious in nature. Enzyme act on substrate molecules and convert to…

Q: What is the percent change for the enzyme active at 40 C compared to 25 C* 220 200 180 160 e…

A: Enzymes are proteins that act as a catalyst to speed up chemical reactions. A catalyst is a…

Q: Why is it important to know the Km and Vmax values of an enzyme

A: An enzyme is a polypeptide molecule made up of amino acids. Amino acids are an organic molecule that…

Q: In _____________ inhibition, the EI complex readily dissociates and the enzyme is again available…

A: Enzyme inhibition refers to a decrease in enzyme-related processes, enzyme production or enzyme…

Q: If 10 µM enzyme was used to obtain the data in the summary plot below, k-cat = ________________…

A: An enzyme is a type of biological catalyst that aids in the acceleration of chemical reactions.…