ENZYMES Flashcards

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1
Q

What is an enzyme?

A

Biological catalysts that speed up the rate of chemical reactions without getting used up by lowering the activation energy of a reaction.

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2
Q

What are enzymes made from?

A

Globular proteins

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3
Q

What is Activation Energy (Ea)?

A

The minimum amount of energy required for a reaction to occur.

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4
Q

What is the affect of enzymes upon the Ea?

A

Lowers Ea allowing the reaction to occur much more easily at a relatively low temp.

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5
Q

What is metabolism?

A

Chemical reactions of an organism

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6
Q

What is catabolism?

A

Breakdown reactions
-binding of substrate induces a conformational change in shape of active site that distorts substrate molecule thus facilitating the breaking of a particular bond

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7
Q

What is anabolism?

A

Build-up reactions

-substrate molecules held on the active site and orientated in a position to facilitate bonding between them.

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8
Q

Explain the Lock and Key Model/Enzyme specificity

A
  1. Active site of an enzyme has a specific complimentary shape (like a lock) into which the substrate (the key) fits into exactly to form the enzyme-substrate complex.
  2. Following the reaction, the product leaves the active site of the enzyme as the shapes are no longer complimentary.
    - this allows the enzyme to be used again
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9
Q

How do enzymes facilitate specificity

A

Each enzyme is specific to a particular substrate (two have a complimentary shape) and follow th lock and key model
-as enzymes are globular, enzymes are able to form a range of 3D shapes needed to facilitate the lock and key model.

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10
Q

Explain the Induced Fit Model.

A
  1. Shape of active site of enzyme is not quite complimentary to shape of substrate
  2. As substrate begins to bind to enzyme, active site moulds itself around substrate making the two complimentary + forming enzyme-substrate complex
  3. Following the reaction, the active site returns to its pre-reaction shape causing the products to leave the active site. (shapes no longer complimentary).
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11
Q

What are cofactors?

A

Non-protein molecules that enzymes require in order to function (e.g Mg2+, Ca2+ and Fe3+)

Attach to enzyme and change the active site enabling substrate to bind and allowing the reaction to occur.

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12
Q

What are prosthetic groups?

A

Type of cofactor that is covalently bonded to enzyme and is integral to function

E.g Haem is a prosthetic group in catalase enzyme

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13
Q

What are coenzymes?

A

Type of cofactor that is not permanently attached to enzyme but is integral to function.

Mostly organic molecules
-NAD and FAD act as Hydrogen acceptors in respiration

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14
Q

What is the effect of substrate concentration on enzyme activity?

A
  1. As substrate conc. increases, enzyme activity increases
    - Greater conc. substrate molecules increases number of successful collisions with active site of enzyme therefore rate of formation of enzyme-substrate complexes (hence activity) increases.
  2. at very high substrate conc., an increase does not cause increase in activity
    - All active sites occupied at any one moment (enzymes fully employed)
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15
Q

Effect of enzyme concentration on enzyme activity?

A
  1. As enzyme conc. increases, enzyme activity increases
    -Greater conc. enzyme molecules increases number of successful collisions with substrate molecules therefore rate of formation of enzyme-substrate complexes (hence activity) increases.
  2. at very high substrate conc., an increase does not cause increase in activity
    -Substrate is limiting factor
    -enzyme is in excess
    N.B- in living organisms, substrate rarely limiting
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16
Q

Effect of pH on enzyme activity?

A

Greater the pH is from optimum, the greater the degree of disruption to ionic bonds in enzyme which causes the shape of the active site to change and enzyme to denature
-Active site no longer complimentary to substrate causing activity to fall.

17
Q

Effect of temp. on enzyme activity?

A
  1. At low temp., an increase in temp. causes an exponential increase in enzyme activity.
    - increase in temp. causes more KE for the successful collision of enzyme and substrate therefore rate of formation of enzyme-substrate complexes (hence activity) to increase.
  2. at optimum temp., enzyme activity at highest
    - greatest rate of enzyme-substrate complex formation
  3. Temp. above optimum, H-bonds in enzyme which causes the shape of the active site to change and enzyme to denature
18
Q

Why do optimum temp. of enzymes differ?

A

Plant enzymes lower optimum than mammalian enzymes

-soil temp. lower than environmental temp. + allow more growth in spring

19
Q

What are enzyme inhibitors?

A

Substances that interfere with enzyme action

- reduce enzyme activity by directly/indirectly affecting active site function

20
Q

what is competitive inhibition?

A

inhibitor has complementary shape to the active site of the enzyme.
Inhibitor competes with substrate to fit into the active site of enzyme and blocks it, reducing the rate of formation of enzyme-substrate complexes (hence activity).
N.B- Reversible

21
Q

what is the affect of conc. on competitive inhibition?

A

substrate conc. > inhibitor conc. = no affect
- most of active sites occupied by substrate
inhibitor conc. > substrate conc. = affect
- most of active sites occupied by inhibitor, therefore enzyme activity decreased

22
Q

Non-competitive inhibition; irreversible inhibitors

A

permanently damages enzyme active site (denature) therefore substrate and active site no longer complimentary causing rate of enzyme-substrate complexes (hence enzyme activity) to decrease.

E.g- Cyanide non-reversible inhibitor of respiratory enzyme cytochrome oxidase

23
Q

Allosteric enzymes

A

enzymes that have a second site which non-competitive inhibitors can attach to to change the shape of the main active site therefore reducing rate of enzyme activity as active site and substrate no longer complimentary.

Inhibitor may leave allowing main active site to regain its catalytic shape

inhibitors used in negative feedback

Increasing conc. of substrate does not have an affect but number of functioning enzymes have been reduced.

24
Q

Angiotensin Converting Enzyme (ACE)

A

• Inhibitors used to treat high blood pressure + other cardiovascular diseases
• Helps prevent high blood pressure by Inhibiting enzyme that leads to a constriction of blood vessels which can cause high blood pressure.
o High blood pressure is a significant factor in many cardiovascular diseases.

25
Q

Penicillin (and other antibiotics)

A

• Inhibits enzymes involved in (peptidoglycan) cell wall formation in bacteria

26
Q

Antiviral drugs

A

• Inhibit DNA/RNA polymerase

o Essential in viral replication

27
Q

Current research

A

• Enzyme inhibitors can be used in the treatment of cancer
• Identifying the shape of active site of enzymes involved in disease progression
o Can model and develop inhibitors with a complimentary shape to block active sites.

28
Q

why does cutting lettuce with a knife cause enzymes to catalyse faster than tearing with hand

A

Cutting results in destruction of cells, so that more enzyme is released;
whereas tearing leaves cells intact/breaks the tissue along cell walls;

29
Q

For enzyme inhibitors to be effective as therapeutic drugs?

A

1) Specific- only bind to enzymes that cause the disease or metabolic pathways may be affected.
- most inhibitors target the complementary and specific active site of the enzyme

2) Be able to work at low doses
- Inhibitors may be toxic at high levels

30
Q

how can enzymes be used as biomarkers of disease?

A

many diseases involve changes in the amounts of biological molecules e.g enzymes in affected tissue

Measurement of these amounts (biomarkers) are useful in diagnosis and monitoring of disease progression

Differences in the levels of enzyme indicate a disease

31
Q

What specimens can enzyme levels be tested?

A

Blood, urine or sputum/phlegm

32
Q

What are biosensors?

A

Devices that use biological material (Enzymes/antibodies) in the detection of a substance of interest.

usually quantitative to identify the conc. of substance of interest.