Unit 1 - Metabolic Pathways Flashcards

1
Q

What are Metabolic Pathways?

A

Metabolic pathways are integrated and controlled pathways of enzyme-catalysed reactions within a cell

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2
Q

What categories are Metabolic Pathways divided into?

A
  1. Catabolism​
  2. Anabolism
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3
Q

Describe Catabolism

A

Catabolic pathways breakdown complex molecules to simple molecules​

This (usually) releases energy

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4
Q

Describe Anabolism

A

Anabolic pathways involve the biosynthesis (build up) of complex molecules from simpler molecules​

This requires energy

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5
Q

What does the use of irreversible steps in metabolic pathways mean?

A

After that point substrates cannot be converted back and are committed to continuing on the pathway

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6
Q

Describe reversible steps in metabolic pathways

A

Reversible steps are important if too much of a substrate builds up​

It allows it to be converted back to the previous substrate​

Some products of metabolism in the body are potentially toxic, this can prevent toxicity

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7
Q

When do you use alternative routes in metabolic pathways?

A

When substrates are plentiful or in short supply

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8
Q

What is the result of Alternative routes in metabolic pathways?

A

This can conserve energy, (or prevent the build-up of toxic intermediate products).​

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9
Q

What controls metabolic pathways?

A

The presence or absence of particular enzymes

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10
Q

What is activation energy?

A

An initial input of energy to start a reaction

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11
Q

Describe the effect of enzymes on activation energy

A

Enzymes reduce Ea, this conserves energy

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12
Q

What is Enzyme Specificity?

A

Enzymes only work with one type of substrate​

The substrate fits exactly into the active site

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13
Q

Name the chemical attraction between substrate and enzyme

A

Affinity

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14
Q

Describe an Induced Fit in Enzymes

A

The active site is flexible and slightly alters its shape when the substrate enters​

This close fit ensures the active site is in very close contact with the substrate

End products are released because there is low affinity with the active site.​

The enzyme will return to its original conformation.

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15
Q

Describe Substrate Orientation

A

In a reaction with 2 or more substrates, the shape of the active site ensure they are held in the correct position​

This weakens the ​chemical bonds

This reduces Ea required to get reactants to ‘transition state’​

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16
Q

Define the Transition State in terms of enzyme activity

A

Transition state is where the structure is no longer a substrate but not yet a product

17
Q

To function efficiently enzymes must have…

A
  • Suitable temperature​
  • Appropriate pH​
    *Adequate supply of substrate
18
Q

Talk about Substrate Concentration in terms of Rates of Reaction

A

Substrate concentration refers to the relative number of substrate molecules present that could bind to an available enzyme. ​

At low concentrations, the rates of reaction in a cell are low because there are too few substrate molecules to bind to active sites of enzymes. ​

An increase in substrate concentration means that there will be more substrate to bind to active sites therefore reaction rate will increase. ​

This trend will continue until all of the active sites are occupied. At this point, enzyme concentration becomes a limiting factor and rates of reaction will plateau.

19
Q

What are the 3 types of Enzyme inhibition?

A
  1. Competitive inhibition​
  2. Non-competitive inhibition​
  3. End-product inhibition
20
Q

Describe Competitive Inhibition

A

Competitive inhibitors compete with a substrate for the active site of an enzyme​

These inhibitors are a similar structure to the substrate so can block an active site

21
Q

Describe Non-Competitive Inhibition

A

Non-competitive inhibitors become attached to a non-active (allosteric) site on an enzyme​

This alters the shape of the enzyme and in turn the active site

22
Q

Describe Allosteric regulation

A

If the allosteric site is occupied by an activator (regulatory molecule) the enzyme will be in an active form​

If occupied by a non-competitive inhibitor, the enzyme will change shape

23
Q

Describe End product inhibition

A

When the end product of an enzyme catalysed reaction builds up it can bind to an enzyme found earlier within the pathway.

This slows down the conversion of A to B, and in turn regulates the whole pathway, preventing wasteful conversion of substrates and accumulation of products​