enzymes Flashcards

(20 cards)

1
Q

What are enzymes?

A

Globular protein biological catalysts that speed up biochemical reactions without being consumed.

Essential for life—working in metabolism, digestion, DNA replication, etc.

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

What is the structure of enzymes?

A

Enzymes have a specific three-dimensional (tertiary) structure due to folding and bonding (hydrogen, ionic, disulfide).

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

What is the active site of an enzyme?

A

A small region that binds substrate(s), forming the enzyme–substrate complex.

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

What is the Lock & Key model of enzyme action?

A

An early model where the enzyme’s active site is rigid and complements the substrate exactly.

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

What is the Induced Fit model of enzyme action?

A

The active site changes shape slightly to fit the substrate when it binds, lowering activation energy.

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

What evidence supports the Induced Fit model?

A

X-ray crystallography showing shape change in enzymes like hexokinase.

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

How do enzymes lower activation energy?

A

By stabilising the transition state, speeding up reactions.

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

What happens to enzymes during chemical reactions?

A

They form and release products, remaining unchanged for reuse.

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

What is enzyme specificity?

A

Each enzyme only catalyses one reaction (or small group) due to the active site’s specific shape and chemistry.

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

Can enzymes be stereospecific?

A

Yes, some enzymes only fit one enantiomer.

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

How does temperature affect enzyme activity?

A

Rate increases with temperature up to an optimum (~37 °C for humans) and denatures above this.

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

What is the Q10 effect in enzymatic reactions?

A

The rate doubles per 10 °C increase until denaturation.

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

What is the effect of pH on enzyme activity?

A

Each enzyme has an optimum pH, and deviations can disrupt structure and reduce activity.

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

What happens to enzyme activity as substrate concentration increases?

A

Rate rises until saturation (Vₘₐₓ), and more enzymes can raise the maximum rate.

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

What are competitive inhibitors?

A

Substrate-like molecules that bind to the active site, reducing enzyme activity.

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

What are non-competitive inhibitors?

A

Molecules that bind elsewhere on the enzyme, reducing activity.

17
Q

How is enzyme activity measured?

A

By tracking substrate decrease or product increase over time.

18
Q

What is the formula for the rate of reaction?

A

Rate of reaction = gradient of concentration vs time graph.

19
Q

What are endopeptidases?

A

Enzymes like pepsin, trypsin, and chymotrypsin that break internal peptide bonds in proteins.

20
Q

What are exopeptidases?

A

Enzymes like dipeptidases that act at the ends of proteins to release amino acids.