It is a model which best explains the enzyme-substrate actionA. lock & keyО в. molecularO c.O D.VSEPRKreb29

Enzymes are biocatalyst that increases the speed of reaction by lowering the activation energy.…

Answered: It is a model which best explains the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

When measuring reaction velocity as a function of substrate concentration, a researcher usually keeps the concentration of enzyme at a constant level. What would happen if the enzyme concentration were not kept constant? A. Vmax would change, but Km would remain constant. B. Both Vmax and Km would change C. Vmax would remain constant, but Km would change D. Vmax would remain constant, but V would change E. None of the above would necessarily occur
2
WriteC if only statement A is correct, H if only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. A competitive inhibitor would bind at the enzyme's active site.B. As a result, the affinity of the substrate to the active site decreases.
The representative reaction of the enzymatic process is:
Which of the following factors affect enzyme activity? a. All of the mentioned answers are correct O b. Substrate concentration Oc. Temperature O d. pH
When an enzyme catalyzes a reaction: onisido stunim q a. Substrate(s) bind in the active site The b. Products bind in the active site eri c. The shape of the enzyme remains unchanged l f d. The enzyme is consumed by the reaction
Label the diagram. d a H,0 C Enzyme- substrate products substrate enzyme active site inhibitor complex a d.
Which of the following is the correct value of the Kö? a. It is [substrate] at half Vmax O b. It is [substrate] at Vmax Oc. It is half of the [enzyme] Od. It is half of the Vmax
There is an enzyme inhibition mechanism that is not too detrimental when viewed from the size of Km, namely the inhibition mechanism.... A. non-competitiveB. non-competitive and uncompetitiveC. in-competitive and uncompetitiveD. in-competitiveE. uncompetitive
Which phrase characterizes a uncompetitive inhibitor? OA. binds either enzyme or enzyme-substrate complex when present, Km of an enzyme will appear to decrease OB. when present, Km of an enzyme will either increase or decrease when present, Km of an enzyme will appear to increase OD.
Which of the following statements about enzyme regulation is NOT true? a. covalent modification is one type of enzyme regulation. b. biologically most important type of regulation is standard inhibition. c. allosteric regulation can involved feedback inhibition. d. some types of enzume regulation are not widely used in biology. e. none of the above
Why does enzyme activity decrease because of pH changes? A. Disruption of hydrogen-bonding interactions between amino acids that are polar-uncharged and charged. B. Disruption of electrostatic interactions between charged amino acids C. Disruption of hydrophobic interactions between nonpolar amino acids. D. Both A and B E. All of these

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It is a model which best explains the enzyme-substrate action O A. lock & key B. molecular OC. VSEPR D. Kreb