Lesson 3.3 - Environmental Impacts on Enzyme Function 𖦹⋆。°✩ Flashcards

1
Q

what can a change to the molecular structure of an enzyme result in

A

may result in a loss of enzyme function

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2
Q

what is the shape of enzymes

A

enzymes have unique 3D shapes known as the conformational shape/tertiary structure

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3
Q

what is denaturation

A

changes in the conformational shape of the enzyme

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4
Q

what can lead to denaturation

A

༻ changes in environmental temperature
༻ changes in environmental pH

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5
Q

what happens when an enzyme is denatured

A

the catalytic ability of the enzyme is lost or severely decreased. denaturation is usually irreversible

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6
Q

in some cases, denaturation is reversible. what happens in this case

A

the enzyme will regain catalytic activity

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7
Q

what can affect the efficiency of enzyme activity and reaction rates

A

༻ environmental temperature
༻ environmental pH
༻ concentration for substrates and products
༻ enzyme concentration

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8
Q

what are optimum temperatures

A

range in which enzyme-mediated reactions occur the fastest

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9
Q

when do reaction rates change with regards to temperature

A

reaction rates change when optimum temperatures aren’t maintained

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10
Q

what happens when there is an environmental increase in temperature

A

༻ initial increase in reaction rates
༻ increased speed of molecular movement
༻ increased frequency of enzyme-substrate collisions

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11
Q

what happens when temperatures increase outside of the optimum range

A

temperature increase outside of optimum range results in enzyme denaturation

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12
Q

what happens when there is an environmental decrease in temperature

A

༻ slowed down reaction rate
༻ decreased frequency of enzyme-reaction collisions
༻ does not disrupt enzyme structure, no denaturation

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13
Q

what does pH measure

A

the concentration of hydrogen ions in solution measured on a logarithmic scale

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14
Q

what do small pH changes equal

A

small changes in PH values equate to large shirts in hydrogen ion concentrations

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15
Q

what is optimum pH

A

the range in which enzyme-mediated reactions occur the fastest

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16
Q

what happens when you change the pH outside of the optimum range

A

enzyme activity will slow/stop
༻ enzyme denaturation can occur as a result of increases/decreases outside of optimum

17
Q

what can changes in hydrogen ion concentration disrupt

A

can disrupt hydrogen bond interactions that help maintain enzyme structure

18
Q

how can concentration of substrates and products affect reaction rate

A

༻ initial increase in substrate concentration increases increase reaction rate because more substrates mean more opportunity to collide with enzymes
༻ increased product concentration decreases opportunity for substrate addition because matter takes up space, so more product in an area means a lower chance of enzyme substrate collisions = slower reaction rate

19
Q

what does substrate saturation result in

A

results in no further increase in rate; reaction rate will remain constant if saturation levels are maintained

20
Q

how does a change in enzyme concentration impact reaction rate

A

༻ less enzyme = slower reaction rate, less opportunity for substrates to collide with active sites
༻ more enzyme = faster reaction rate, more opportunity for substrates to collide with active sites

21
Q

what do competitive inhibitors bind to

A

the active site

22
Q

what are competitive inhibitors

A

molecules that can bind reversibly/irreversibly to the active site of the enzyme

23
Q

what do competitive inhibitors do

A

competes with the normal substrate for the enzyme’s active site

24
Q

what happens if the inhibitor concentrations exceed substrate concentrations

A

reactions are slowed

25
what happens if inhibitor concentrations are significantly lower than substrate concentrations
reactions can proceed normally
26
what happens if inhibitor binding is irreversible
enzyme function will be prevented
27
what happens if inhibitor binds reversibly
enzyme can regain function once inhibitor detaches
28
can molecules only bind to the enzyme's active site
no, enzymes have regions other than the active site to which molecules can bind
29
what are these alternate sites called
allosteric sites
30
what are noncompetitive inhibitors
༻ do not bind to active site, bind to allosteric site
31
what does binding to the allosteric site cause
binding causes conformational shape change and prevents enzyme function because the active site is no longer available
32
what can increasing substrate NOT do
cannot prevent effects of noncompetitive inhibitor binding