Enzymes - Rate of Reaction Flashcards

1
Q

what is the effect of increasing temperature

A

increases the rate of reaction due to increasing kinetic energy of the molecules. there are therefore more collisions between molecules.

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

explain collision theory

A
  • substrate must collide with active site of enzyme with enough force for reaction to occur.
  • if the kinetic energy of both molecules is increased by heating, there are more collisions with more force
  • leading to a higher rate of reaction and more product formed.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what is the unit of rate of reaction

A

s^-1

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

what is the formula for rate of reaction

A

1/time taken to reach end point

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

what is the temperature coefficient

A

the increase in the rate of a process when the temperature is increased by 10 degrees

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

what is the formula for temperature coefficient

A

Q10 = rate of reaction at (T+10) degrees/ rate of reaction at T degrees

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

what is the optimum temperature

A

the temperature that gives the enzyme’s maximum rate of reaction

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

what happens when the bonds in the tertiary structure are broken by increased kinetic energy and vibrations

A

denaturation

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

what is denaturation

A

where the tertiary structure of the enzyme is changed to the point that the enzyme no longer works

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

is denaturation reversible

A

no

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

how can temperature cause denaturation

A
  • increased kinetic energy makes the molecules vibrate, breaking the weaker hydrogen and ionic bonds
  • these bonds are vital in maintaining the tertiary structure and hence the shape of the active site
  • rate of reaction decreases, and if enough bonds are broken the whole tertiary structure will unravel
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what is pH

A

a measure of the hydrogen ion concentration

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

what do hydrogen ions affect

A

the ionic and hydrogen bonds in the tertiary structure

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

how does pH affect the tertiary structure of protein

A
  • the active site relies on charged R-groups of the amino acids that make up the active site in order for enzyme to function
  • H+ ions are attracted to negatively charged groups and cluster around them. Interferes with binding of substrate to active site
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

define optimum pH

A

the pH that gives the enzyme’s maximum rate of reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

does denaturation always occur when pH changed below or above optimum

A

no, minor changes do not denature enzymes. The bonds that are disrupted can reform if pH returns towards optimum

17
Q

how does substrate concentration affect rate of reaction

A

as concentration of substrate increases, collisions with enzymes become more frequent, more product is made and rate of reaction increases
eventually, rate reaches a maximum as all active sites are occupied at all times so any further increase in substrate conc. has no effect

18
Q

how does enzyme concentration affect rate of reaction

A

increased enzyme concentration increases rate as there are more frequent collisions between enzymes and substrates, rate will reach a maximum eventually if substrate concentration remains fixed.