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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what is the shape of enzymes

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what is denaturation

A

changes in the conformational shape of the enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what can lead to denaturation

A

༻ changes in environmental temperature
༻ changes in environmental pH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

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

A

the enzyme will regain catalytic activity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what are optimum temperatures

A

range in which enzyme-mediated reactions occur the fastest

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

when do reaction rates change with regards to temperature

A

reaction rates change when optimum temperatures aren’t maintained

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what happens when temperatures increase outside of the optimum range

A

temperature increase outside of optimum range results in enzyme denaturation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what does pH measure

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

what do small pH changes equal

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what is optimum pH

A

the range in which enzyme-mediated reactions occur the fastest

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
Q

what happens if inhibitor concentrations are significantly lower than substrate concentrations

A

reactions can proceed normally

26
Q

what happens if inhibitor binding is irreversible

A

enzyme function will be prevented

27
Q

what happens if inhibitor binds reversibly

A

enzyme can regain function once inhibitor detaches

28
Q

can molecules only bind to the enzyme’s active site

A

no, enzymes have regions other than the active site to which molecules can bind

29
Q

what are these alternate sites called

A

allosteric sites

30
Q

what are noncompetitive inhibitors

A

༻ do not bind to active site, bind to allosteric site

31
Q

what does binding to the allosteric site cause

A

binding causes conformational shape change and prevents enzyme function because the active site is no longer available

32
Q

what can increasing substrate NOT do

A

cannot prevent effects of noncompetitive inhibitor binding