Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

Factors affecting rate of enzyme controlled reactions

A

Substrate / enzyme concentration, pH, temperature, presence of inhibitors / activators

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

Explain induced fit model

A

Substrate collides with active site, activesite changes shape to fit substrate better which puts strain and pressure on bonds within substrate lowering activation energy ESC form + then so do EPCs and active site return to normal shape and product released

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

Explain relationship between rate of reaction and increasing temperature

A

① Initially ROR increases exponentially as temp increases to optimum because increase in kinetic energy = increase in successful collisions = more escs form and active site of enzyme will change shape as
molecules vibrate more so that it becomes better fit
② optimum temp → highest ROR because active site of enzyme is perfectly complementary to substrate so highest number of successful collisions and production is at max rate
③ ROR reduces rapidly until no more because when temp >optimum then vibrations in molecules are so great that breaks hydrogen bonds holding different parts of protein together altering specific shape of active site so no longer complementary to substrate + progresses as temp ↑

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

Example of induced fit

A

Lysozyme

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

Explain relationship between ROR and pH

A

At optimum pH, ROR is highest because charges of active site and substrate and shapes are complementary so attracted to each other
As pH moves away from optimum, ROR declines because 3D shape of enzyme and therefore its active site is distorted by breaking of hydrogen and ionic bonds so active site and substrate no longer complementary and charges between enzyme and active site changed due to free H plus and hydroxide ions so-enzyme and substrate repel each other so fewer successful collisions. ( if active site has you many h plus ions, could repel each others )

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

Define ph

A

Measure of h+ ions concentration

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

What happens if enzyme becomes more acidic

A

H plus ions bond to the negative charges on active site making them positive so no longer complementary to substrate + repels it

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

What is an immobilised enzyme

A

Enzyme fixed in mert material

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

Ways to immobilise an enzyme

A

Alginate beads, gel membrane, meshwork of in ent material, stuck to polyethene..

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

Effect of immobilising enzymes

A

Stabilises enzyme and widens its optimum range and stable at higher temps because

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

What is a catalyst

A

Biological molecule which can speed up reaction without being used up or changing products by providing alternate reaction path with lower activation energy so reactions can occur at low temperature

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What does it mean in terms of quaternary structure that enzymes are globular proteins

A

Multiple polypeptides bonded together and each polypeptide chain folded into 3D structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is activation energy

A

Minimum amount of Extra energy required to enable reaction to start

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

Why is tertiary structure of enzyme essential to its function

A

. Tertiary structure determines shape of active site which is only complementary to specific substrate so change in active site shape means that enzyme cannot catalyse reaction

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

What does enzyme actually do when it breaks apart a substrate

A

Hydrolysis with breaking of… Bond

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

Explain lock and key model

A

Shape of active site of enzyme is specific and complementary to substrate so they fit perfectly together like key in lock and bind together and enzyme substrate complex formed and products released and active site never changes shape

16
Q

Why is induced fit model preferred over lock and key

A

Enzymes aren’t rigid structures and enzyme - substrate complex changes shape slightly and ensures tighter bonding in active site

17
Q

What happens to enzymes when temp is too high

A

Enzymes denature because hydrogen bonds in tertiary structure break so shape of active site changes so enzyme no longer functions

18
Q

What are 2 characteristics of enzymes

A

Reusable and shape of active site remains unchanged

19
Q

Difference between intracellular and extra cellular enzymes

A

Intracellular = inside cell
Extracellular = outside cell

20
Q

Explain effect of substrate concentration on ROR.

A

ROR increases steadily as substrate concentration increases because more successful collisions so more enzyme substrate complexes form + more product made → ROR plateaus even as substrate concentration increases because every enzyme working at maximum rate and maximum tum over number so active site is continually filled and increasing substrate concentration has no effect

21
Q

Explain effect of enzyme concentration on ROR when substrate is in excess

A

As enzyme conc increases, ROR increases linearly because more active sites available so more successful collisions between active site and substrate so more enzyme - substrate complexes form so more product each minute → continues as long as substrate in excess

22
Q

Purpose of buffer

A

Maintain pH otherwise pH could affect rate of reaction, denature enzymes or to help keep pH at optimum for max ROR

23
Q

Explain non- competitive inhibitor

A

Don’t compete for active site with substrate → instead binds to allosteric site distorting tertiary shape of enzyme to active site shape change so substrate no longer complementary and can’t fit so enzyme-substrate complexes can’t form so ROR decreases and maximum rate of enzyme activity is reduced → binding is usually irreversible but ones involved in control of metabolic pathway are reversible

24
Q

Effect of substrate conc on level of inhibition by non competitive inhibitor

A

No effect because substrate no longer fits → isn’t complementary

25
Q

Example of non competitive inhibitor

A

Cyanide ions → respiratory inhibitor → inhibit cytochrome oxidase enzymes

26
Q

2 types of reactions enzymes catalyse

A

Anabolic → condensation of smaller molecules making large molecules
Catabolic → breaking down / hydrolysis of larger molecules to smaller molecules