Draw the Lock and Key and Induced-Fit Models of enzyme-substrate complex

Q: Under the following conditions, fill in the blanks. Then, describe why this inhibitor is the type of…

A: Enzyme inhibition refers to the decrease in enzyme related process which may be enzyme production or…

Q: As more inhibitor is added to the enzyme reaction depicted in the graph below, the shift in the…

A: Enzymes are high molecular weight proteins that catalyse biochemical reactions. They contain an…

Q: Classify each specific inhibitor or inhibitor characteristic according to one of two types of…

A: Enzymes are biocatalysts that are made up of amino acids that means they are proteinaceous in…

Q: Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single…

A: The reactants must overcome a kinetic barrier to proceed with the conversion to products in every…

Q: B A Which sketches represent the action of an enzyme? Check none of them if none of them do. B And…

A: There are three sketches 1, 2 and 3 with labelling A, B and C. We need to identify the enzyme action…

Q: The characterization of an enzyme usually includes the determination of key kinetic parameters.…

A: vo: initial rate of reaction or rate of reaction when all the enzyme is yet to be saturated with…

Q: What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is…

A: The relationship between Km and substrate concentration is that Km corresponds to the substrate…

Q: what would the km and kcat look like in a perfect enzyme

A: In a perfect enzyme, the rate of the catalyzed reaction would be limited only by the rate at which…

Q: Match each statement with the condition that it describes.

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

Q: Describe the induced-fit model of enzyme activity.

A: There are different models that explain the binding of enzymes and substrates and the mechanism…

Q: In the following example an enzyme is being inhibited. This is an example of Active site Inhibitor…

A: The active site of an enzyme is specialized for substrate binding. Whereas in the allosteric site,…

Q: Match the descriptions and compounds with the terms competitive, uncompetitive, and noncompetitive…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Q: Explain the Jacques Monod, Jeffries Wyman and Jean-Pierre Changeux (or MWC) model for allosteric…

A: Enzymes are biocatalysts, which increase the rate of biochemical reactions. Substrate molecules bind…

Q: Distinguish between the concerted and sequential models for the behavior of allosteric enzymes.…

A: Allosteric enzymes are those enzymes that change their conformation upon binding to a molecule other…

Q: Enzyme X has a Km of 2 µM and a kcat of 104 s1. In the presence of an inhibitor, Km increases to 4…

A: Enzymes are protein molecules that speed up the reactions by decreasing the activation energy.…

Q: The Michaelis-Menten equation is often used to describe the kinetic characteristics of an…

A: Enzymes are known as biological catalysts, which accelerate the rate of the reaction without…

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: Using the binding of enzyme and ligand, DESCRIBE protein-protein interaction in biological systems.…

A: Enzymes are biological catalysts that enhance the rate of reactions happening inside our body.…

Q: Calculate 1/[S] and 1/V to complete the table. Use this data to draw a Lineweaver-Burke plot, with…

A: A Lineweaver-Burk plot represents the relationship between the reciprocal values of substrate…