Metabolism Flashcards

1
Q

What is glycolysis?

A

The conversion of glucose into pyruvate.

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2
Q

How do enzymes speed up reactions?

A

Enzymes speed up reactions by lowering the activation energy..

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3
Q

What happens in the link reaction?

A
  • Pyruvate is decarboxylated, Carbon is removed in the form of CO2.
  • NAD is reduced to become NADH
  • This convert pyruvate to Acetyl CoA.
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4
Q

What is the net gain of ATP and reduced NAD in glycolysis?

A

2 ATP & 2 NADH

2 ATP is used and 4 is produced

2 NADH is produced.

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5
Q

Explain what happens in glycolysis?

A
  • Glucose is phosphorylated by adding 2 phosphates, the result is 2 molecules of triose phosphate.
  • Triose phosphate is oxidized as it loses hydrogen, the result is pyruvate.
  • NAD collects the 2 hydrogen ions to form 2 NADH.
  • 4 ATP is produced. (Net gain od 2 ATP)
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6
Q

Where does the krebs cycle take place?

A

In the Matrix of the mitochondria

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7
Q

Explain what happens in the krebs cycle?

A
  • Acetyl CoA (2C) reacts with Oxaloacetate (4C) to form citrate (6C).
  • Acetyl CoA goes back to the link reaction to be used again.
  • Decarboxylation occurs, 6C Citrate becomes a 5 carbon compound (a-ketoglutarate).
  • Decarboxylation occurs again, 5 carbon compound becomes 4 carbon compound.
  • 2 NAD’s gets reduced.
  • ATP is produced.
  • FAD is reduced
  • The end product is oxaloacetate, which is used again to do the same cycle.
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8
Q

What are the types of inhibitors?

A
  1. Competitive inhibitor
  2. Non-competitive inhibitor
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9
Q

What does the competitive inhibitor do?

A

Competes with the substrate for the same active site.

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10
Q

What does the non-competitive inhibitor do?

A

Bind at a different site which alters(affects) the shape of the enzyme.

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11
Q

How can the rate of reaction be increased in competitive inhibition?

A

By increasing the number of substrates, because there is more available substrate than inhibitors.

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12
Q

What are some differences between competitive and non-competitive inhibition?

A
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13
Q

What is end-product inhibition?

A

When the end-product of a reaction allosterically inhibits the first enzyme from starting another reaction.

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14
Q

What is an allosteric site?

A

A binding site on the surface of an enzyme other than the active site. It is also the site where the end-products binds to in an end-product inhibition.

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15
Q

Explain the example of isoleucine and threonine.

A
  • Threonine is turned into isoleucine through the help of different enzymes.
  • Isoleucine is the final product, which then binds allosterically to the enzyme that catalyses the first step, which means that the substrate can no longer bind to the active site.
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