C1.1 Enzymes Flashcards

1
Q

C1.1.1 Enzymes as catalysts

A

A catalyst:
* increases the rate of a chemical reaction
* is not changed by the reaction
* can catalyse a reactions many times

Enzymes = biological catalysts. They are made by living cells to speed up biochemical reactions.

Substrate(s) + enzyme(s) → product(s)

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2
Q

C1.1.2 Role of enzymes in metabolism

A

Almost all metabolic reactions are catalysed by an enzyme. Enzymes catalyse specific/group (of) reaction.

This allows organisms to control metabolism, as making more/less of an enzyme, cells control rate of a reaction.

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3
Q

C1.1.3 Anabolic reactions

A

Anabolic reactions use energy from ATP to produce macromolecules from monomers. They are condensation reactions.

  • protein synthesis (translation) by ribosomes
  • photosynthesis
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4
Q

C1.1.3 Catabolic reactions

A

Catabolic reactions break down larger molecules into smaller ones, releasing energy. This energy can be captured by coupling the reaction to ATP synthesis.
* digestion of food
* cell respiration

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5
Q

C1.1.4 Enzymes as globular proteins with an active site for catalysis

A
  • Enzymes are globular proteins.
  • substrate(s)+ active site shape and chemical properties match each other.

Active site amino acids are often apart in the PP but brought together by folding. 3D structure = crucial; alteration may change AS + prevent catalysis.

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6
Q

C1.1.5 Interactions between substrate and active site to allow induced-fit binding

A

The substrate binds, altering bond angles and lengths of S + AS in induced-fit binding.

Changes to substrate(s) make it easier for bonds within them to break/form.

Product(s) detach, active site to return to its original state and repeats the catalytic cycle.

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7
Q

C1.1.6 How do substrate-active site collisions occur?

A

Substrates and enzymes move randomly. When close enough to interact, the E’s chemical properties attract S to AS. Substrate–active site collision occurs = binding.

Happens more w/ higher substrate/enzyme concs or inc temperature.

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8
Q

C1.1.6 How does molecular motion vary between substrates and enzymes?

A
  • In cytoplasm: both are dissolved = free to move. Often, substrate is smaller, moves more.
  • Substrates = large, don’t move much. Enzyme moves in relation to substrate (transcribe DNA).
  • Enzymes embedded in membranes = immobilized. Substrate does the movement.
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9
Q

C1.1.7 Relationships between the structure of the active site, enzyme–substrate specificity and denaturation

A

This is called Enzyme–substrate specicity allows specific binding. Enzyme’s 3D shape is determined by AA interactions, affected by heat/acidity. AS changes can prevent substrate catalysis + denaturation.

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10
Q

C1.1.8 Effects of temperature on the rate of enzyme activity

A

Liquid is heated→particles gain kinetic energy. Enzyme + substrate molecules move quicker, collision chance increases.

Heating enzymes = bonds to vibrate more, increasing chance of bond breakage. Alters active site → denaturation.

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11
Q
A
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