2.4. 1 Enzymes Flashcards

1
Q

Active Site:

A

Intended area on the surface of an enzyme molecule with a shape that is complementary to the shape of the substrate molecule

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2
Q

Catalyst

A

chemical that speeds up the rate of a reaction and remains unchanged and reusable at the end of the reaction.

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3
Q

Extracelluar

A

outside of the cell

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4
Q

Intracellular

A

inside of the cell

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5
Q

Product

A

molecule produced from substrate molecule, by an enzyme-catalysed reaction

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6
Q

substrate

A

molecule that is altered by an enzyme catalyzed reaction

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7
Q

Why are enzymes remarkable?

A
  1. Enzymes are more specific than chemical catalysts. They do not produce unwanted by-products and rarely make mistakes.
  2. Cells in which they are made can also regulate their production and activity to fit the needs of the cell or organisms at the time.
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8
Q

Enzyme structure determines function

A
  1. For enzymes to catalyse some reactions they may need help from some Cofactors
  2. Instructions for making enzymes are encoded in genes. If the gene has a mutation that alters the sequence of amino acids in the protein, then this may alter the enzyme’s tertiary structure and prevent it from functioning
  3. If an enzyme that catalyses a metabolic reaction is deficient then a metabolic disorder results
  4. Enzymes also catalyse the formation of the organism;s structural components such as collagen in bones, cartilages.
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9
Q

Catabolic

A

metabolites are broken down to smaller metabolites

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10
Q

What are metabolites?

A

Reactants, intermediates, products

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11
Q

What are anabolic pathways

A

energy is used to synthesise large molecules

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12
Q

What does catalase consist of

A

Four polypeptide chains and contains a haem group with iron.

  • Fastest acting enzyme, having the highest turnover
  • Eukaroytic cells, catalase is found inside small vesicles called peroxisomes
  • When white blood cells ingest pathogens they use catalase to help kill invading microbes
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13
Q

Amylase

A
  1. Salivary glands and acts in the mouth to digest the polysaccharide starch to the diasccahride maltose.
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14
Q

What is a Cofactor

A
  1. a substance that has to be present to ensure that an enzyme-catalysed reaction takes place at the appropriate rate.
  2. A cofactor that is permanently bound, by covalent bond is called a prosthetic group
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15
Q

Example of a Cofactor

A
  • Carbonic anhydrase contains a zinc ion permanently bound.

- Found in erythrocytes and catalyses the interconversion of co2 and water to carbonic acid

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16
Q

Induced fit hypthoseis

A
  1. Enzyme specificity
  2. When substrate molecules fit into the enzymes active site, the active site changes shape slightly to mould itself around the substrate molecule.
  3. The active site is still complementary to the shape of the molecule but when binding, there is a subtle change of shape of the side chains that give the active site more conformation.
  4. Moulding enables the substrate to bind more effectively to the site
  5. Non covalent forces
    5.