/*! This file is auto-generated */ .wp-block-button__link{color:#fff;background-color:#32373c;border-radius:9999px;box-shadow:none;text-decoration:none;padding:calc(.667em + 2px) calc(1.333em + 2px);font-size:1.125em}.wp-block-file__button{background:#32373c;color:#fff;text-decoration:none} Q10CP What distinguishes an inhibitor ... [FREE SOLUTION] | 91影视

91影视

What distinguishes an inhibitor from an inactivator?

Short Answer

Expert verified

Inhibitors reduce the activity of an enzyme while inactivators permanently block the activity of an enzyme.

Step by step solution

01

Inhibitors

Many compounds affect an enzyme's activity by interacting with it to affect its substrate binding and turnover number,resulting in reduced enzyme activity. These substances are known as Inhibitors.

Inhibitors reduce enzymes activity by binding reversibly with the enzyme. Some inhibitors are compounds structurally similar to the substrates of respective enzymes but do not react with them or react extremely slowly. Other inhibitors affect enzymatic activity by binding to the enzyme-substrate complex. Many inhibitors do both.

02

Inactivators

Inactivators function through several different mechanisms.Inactivators, also known as irreversible enzyme inhibitors, attach to an enzyme so strongly that they prevent it from functioning permanently.

03

Explanation

Inhibitors reversibly bind to the enzymes to diminish their activity, while inactivators bind irreversibly to the enzymes.

Unlock Step-by-Step Solutions & Ace Your Exams!

  • Full Textbook Solutions

    Get detailed explanations and key concepts

  • Unlimited Al creation

    Al flashcards, explanations, exams and more...

  • Ads-free access

    To over 500 millions flashcards

  • Money-back guarantee

    We refund you if you fail your exam.

Over 30 million students worldwide already upgrade their learning with 91影视!

One App. One Place for Learning.

All the tools & learning materials you need for study success - in one app.

Get started for free

Most popular questions from this chapter

Estimate KI for a competitive inhibitor when [I] = 5mM gives an apparent value of KM that is three times the KM for the uninhibited reaction.

Sphingosine-1-phosphate (SIP) is important for cell survival. The synthesis of SIP from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below.

[Sphingosine]

(饾泹惭)

v鈧 (mg min鈦宦)

(no inhibitor)

v鈧 (mg min鈦宦)

(with threo-sphingosine)

2.5

32.3

8.5

3.5

40

11.5

5

50.8

14.6

10

72

25.4

20

87.7

43.9

50

115.4

70.8

Construct a Lineweaver-Burk plot to answer the following questions:

(a) What are the apparent KM and Vmax values in the presence and absence of the inhibitor?

(b) What kind of an inhibitor is threo-sphingosine? Explain.

For an enzyme-catalyzed reaction, the presence of 5 nM of a reversible inhibitor yields a Vmax value that is 80% of the value in the absenceof the inhibitor. The KM value is unchanged. (a) What type of inhibition is likely occurring? (b) What proportion of the enzyme molecules have bound inhibitor? (c) Calculate the inhibition constant.

You are attempting to determine KM by measuring the reaction velocity at different substrate concentrations, but you do not realize thatthe substrate tends to precipitate under the experimental conditions youhave chosen. How would this affect your measurement of KM?

List some advantages of phosphorylation/ dephosphorylation cascade systems over simple allosteric regulation.

See all solutions

Recommended explanations on Biology Textbooks

View all explanations

What do you think about this solution?

We value your feedback to improve our textbook solutions.

Study anywhere. Anytime. Across all devices.