Biology  by Bradford
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3.2 Environmental Impacts on Enzyme Function: revision map

The subtopic in the middle and four tasks round it: label two diagrams, complete a table and fill 13 gaps. Every box rests on a learning objective of the topic in the AP Biology course and exam description. Type into the blanks and check them, or print it on A4, Letter or A3 with an answer key.

Unit 3 practice questionsThe whole Unit 3 map

Topic 3.2

Environmental Impacts on Enzyme Function

AP Biology ยท Unit 3 Cellular EnergeticsName

3.2.AFactors that change the rate

FactorEffect on rateWhy
Temperature rising toward the optimummore collisions between enzyme and substrate
Temperature far above the optimumthe enzyme is : weak bonds break and the active site changes shape
pH away from the optimumfallscharges on R groups change, altering the shape
More substraterises, then plateausall active sites are in use: the enzyme is saturated

3.2.ARate and temperature

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Topic 3.2Environmental Impacts on Enzyme Function

3.2.BTwo kinds of inhibitor

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3.2.BInhibitors and regulation

A inhibitor resembles the substrate and blocks the active site, so adding more substrate can overcome it. A noncompetitive inhibitor binds at another place, the site, and changes the shape of the active site, so extra substrate cannot overcome it. Cells use this to switch pathways off: in feedback inhibition the end product of a pathway inhibits an enzyme near its start, so the cell does not make more than it needs.

Word bank allostericallosteric sitecompetitivecompetitive inhibitordenaturationdenaturedenzymefallsmore collisionsnoncompetitive inhibitoroptimum temperaturerisestemperature

Answer key

Every box on the sheet with its gaps filled in, as the subtopic reads in full.

  1. LabelRate and temperature

    1. optimum temperature
    2. more collisions
    3. denaturation
    4. temperature

  2. LabelTwo kinds of inhibitor

    1. competitive inhibitor
    2. enzyme
    3. noncompetitive inhibitor
    4. allosteric site

  3. TableFactors that change the rate

    FactorEffect on rateWhy
    Temperature rising toward the optimumrisesmore collisions between enzyme and substrate
    Temperature far above the optimumfallsthe enzyme is denatured: weak bonds break and the active site changes shape
    pH away from the optimumfallscharges on R groups change, altering the shape
    More substraterises, then plateausall active sites are in use: the enzyme is saturated

  4. GapsInhibitors and regulation

    A competitive inhibitor resembles the substrate and blocks the active site, so adding more substrate can overcome it. A noncompetitive inhibitor binds at another place, the allosteric site, and changes the shape of the active site, so extra substrate cannot overcome it. Cells use this to switch pathways off: in feedback inhibition the end product of a pathway inhibits an enzyme near its start, so the cell does not make more than it needs.