Molecules: Enzymes And Metabolism Flashcards

1
Q

What is anabolism

A

Synthesis of complex molecules from simpler molecules

Requires input of energy

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2
Q

What is catabolism?

A

Breakdown of complex molecules into simpler molecules (e.g. hydrolysis)

Energy is released

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3
Q

Describe the structure of a catalyst

A

Active site formed by folding of polypeptide chain(s)

Resulting 3D shape forms the active site, where substrate interacts with enzyme

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4
Q

What is collision theory?

A
  1. Particles must collide to react
  2. Must have sufficient energy to break and make new bonds
  3. Must collide at the correct orientation
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5
Q

What is the induced fit model?

A

Active site undergoes a slight change in shape to tighter fit the substrate (lock and key)

Enzyme then induces weakening of bonds thus reducing activation energy needed for reaction

Goes back to its original shape after releases products

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6
Q

How does Denaturation destroy enzyme function?

A

Destroys tertiary/quaternary conformation of protein

Occurs due to: extreme temp, pH, heavy metal

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7
Q

Activation energy and transition state

A

Activation energy is minimum amount of energy needed to reach transition state in which bonds in substrate are broken

Enzymes help lower activation energy (MODS)

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8
Q

What are the 3 factors affecting enzyme concentration?

A

Temp
pH

Substrate concentration
Enzyme concentration

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9
Q

What happens when pH is extreme?

A

Will alter 3D structure of its active site:

Affects charges on amino acid molecule=no more attraction between amino acids—> Denaturation

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10
Q

Intracellular enzyme-catalysed reactions

A

Metabolic reactions in cell catalysed by enzymes produced by free ribosomes

Glycolysis—>cytoplasm
Krebs cycle—>mitochondria

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11
Q

Extracellular enzyme-catalysed reactions

A

Outside cell, catalysed by enzymes produced by bound rbibosomes and secreted outside cell by exocytosis

Lipase, protease, amylase in gut

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12
Q

Explain the generation of heat by metabolic reactions

A

2nd law thermodynamics no energy transformation is 100% efficient

Some energy is always lost in metabolic reaction and used to maintain constant body temp in warm blooded mammals

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13
Q

Competitive vs non-competitive inhibition

A

Competitive: inhibitor competes w substrate to bind to active site (increase in substrate conc.=reduced inhibitor rate) chemically similar to substrate

Non-competitive: inhibitors bind to allosteric site (away from active site) altering enzyme shape, increase in conc. no effect

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14
Q

Example or competitive & non-competitive inhibition

A

Statin drugs competitive lower cholesterol levels (inhibit enzyme HMG-CoA that plays role in cholesterol synthesis)

Hexokinase role in glucose metabolism. Glucose-6-phosphate a product of hexokinase activity can bind to allosteric site of hexokinate and regulate glucose metabolism in brain

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15
Q

What is end-product inhibition?

A

Where end-product of reaction acts as non-competitive inhibitor (e.g. hexokinase)

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16
Q

Mechanism based inhibition

A

Inhibitor binds permanently to active site—> produces stable inhibitor eb]nzyme complex= no catalytic activity

Harmful to organisms e.g. penicillin weakens cell wall of bacteria, wall bursts