Enzymes Flashcards

1
Q

What are enzymes?

A

Enzymes are biological enzymes which catalyse specific chemical reactions.

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2
Q

What are the different functions of the enzyme?

A
  • Digestion of carbohydrates,fats and proteins
  • Blood Clotting
  • Defense i.e. the immune system
  • Movement
  • Nerve Conduction
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3
Q

What two types of enzymes are there?

A

Extracellular or Intracellular

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4
Q

What are the names of the specifc types of enzymes that catalyse specific reactions?

A
  • nucleases
  • proteases
  • polymerases
  • kinases
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5
Q

What is an issue of an enzyme having a defect?

A

They can cause disease such as phenylketonuria (a disease where-by the Phe cannot be turned inro Tyr

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6
Q

Antibiotics, anti-inflammatory and anticancer drugs are all use enzymes as…?

A

A drug target. For example, antibiotics such as penicillin can inhibit cell wall synthesis, anti-inflammatory agents such as asprin blocks prostaglandins and anticancer drugs such as methotrexate, a folate analouge that interferes with the synthesis with DNA precusors.

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7
Q

What are the key properties for enzymes?

A
  • increase the rate of reaction up to 10 billion fold
  • are specific
  • remain unchanged at the end of a reaction and do not alter the equlibrium position
  • facilitate the reaction by decreasing the amount of free energy is needed by the reaction
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8
Q

How does the enzyme bind to the substrate?

A

The enzyme has a 3D cleft, also known as the active site, which binds to the substrate using electrostatic, hydrophobic, hydrongen bonding and van der Waals interactions creating binding energy which helps reduce the amound of free energy needed.

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9
Q

How can you prove the existence of active sites?

A

From x-ray crytallography and kinetic studies of enzyme acitivty.

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10
Q

What is the lock and key model?

A

The lock-and-key model states that the substrate acts as a ‘key’ to the ‘lock’ of the active site. The active site and substrate are exact matches for each other, similar to puzzle pieces fitting together. In this model, only a single substrate is the precise match for the enzyme. Once the enzyme finds its exact counterpart, the chemical reaction can begin.

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11
Q

What is the induced fit model?

A

The induced-fit model is generally considered the more correct version. This theory maintains that the active site and the substrate are, initially, not perfect matches for each other. Rather, the substrate induces a change of shape in the enzyme creating an even tighter fit than before.

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12
Q

How can the evidence for the induced fit model be created?

A

Through crystallising enzymes before and after being bound to a substrate in order to see if the shape has chnanged.

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13
Q

What type of energy is used to catalyse the reaction?

A

Enzyme-substrate binding energy, soenergy gained from bringing the reactants together which is also known as approximation. This can increase the rate of reaction.

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14
Q

What can the binidng enery do?

A
  • Increase the rate of reaction
  • Constrain the movement of the substrate when it is bound
  • Stabilise positive and negative charges in t-state (this means that the enzyme will have residues which neutralise the charges that pop up during transition)
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15
Q

What other method are enzymes able to do in order to speed the rate of the reaction up?

A

They can find an alternative reaction pathway which requires less energy, which means that more molecules are able to to have required activation energy and thus more frequent collisions and then an increase in the frequency of successful collisions, so a faster rate of reaction.

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16
Q

Why is it useful for the enzyme to strain bonds within the enzyme?

A

By straining particular bonds within the enzyme as well as lowering the activation energy needed, it makes it easier for the substrate to be broken down since straining the bonds can distort the shape of the substrate into its transition state.

17
Q

What can enzymes use to help bring substrates to its active site?

A

Co-factors.

18
Q

What can enzymes exclude from its active site to make the reaction of breaking down the substrate faster?

A

Solvents.

19
Q

What is reaction velocity?

A

The rate at which products are made from the substrate.

20
Q

What is Vmax?

A

It is the maximum possible velocity when all active sites are occupied- this can be represented on a graph where the curve plateaus off.

21
Q

What is Vmax2?

A

The maximum possible velocity when half of all active sites are occupied - this is exactly half of the Vmax.

22
Q

What does it mean when on a velocity concentration graph’s line plateaus off?

A

It shows that the limiting factor are the active sites, as there is a limit to how much it can increase by.

23
Q

What is Km?

A

It is the amount of substrate that you would have to put in to half saturate the active site (this helps to show the binding affinity of the enzymes).

24
Q

What is the formula for the enzyme reaction (Michaelis-Menten equation)

A

E + S ↔ ES ↔ E + P

Where E is the enzyme, S is the substrate, ES is the enzyme-substrate complex, and P is the product.

25
Q

How can you calculate the velocity (V)?

A

V = Vmax + [S]/Km + [S]

1/V= 1/Vmax + Km/Vmax * 1/[S]

26
Q

What does having a high Km value mean and what does having a low Km value mean?

A

Having a high Km value means that the enzyme has a low binding affinity for its substrate and if an enzyme has a low Km value it means that the enzyme has a high binding affinity for its substrate.

27
Q

What does competitive inhibition mean?

A

Where both the inhibitor and the substrate can bind to the active site.

28
Q

How is Vmax and Km affected if a competitive inhibitor is added?

A

Vmax does not change however Km increases which means that the reaction can reach its full velocity but to get to half of the Vmax, it will need much more substrate to outcompete the inhibitor.

29
Q

What does non-competitive inhibition mean?

A

The inhibitor binds to a different active site to the substrate.

30
Q

How is Vmax and Km affected if a non-competitive inhibitor is added?

A

Vmax decreases and the Km remains unaltered as there are less active sites available so it takes longer for the substrate to react however the affinity for the active sites has not changed.

31
Q

What are the ways that enzymes have their activity regulated?

A
  • Gene expression
  • Compartmentation
  • Allosteric regulation
  • Covalent modification
32
Q

What is compartmentation?

A

Where the sequence on the enzyme polypeptide chain are scanned and tells the enzyme where to go i.e nucleus, ER etc.

33
Q

What is allosteric regulation?

A

Regulatory molecules which control the shape of the protein and can increase or decrease enzyme activity.

34
Q

What is covalent modification?

A

Changing the shape of the enzymes by altering its bonds which also affects its activity.

35
Q

What is feedback inhibition?

A

The end product of a metabolic pathway acts on the key enzyme regulating entry to that pathway, keeping more of the end product from being produced.

36
Q

Explain what occurs in feedback inhibition.

A

A becomes inhibited by Z
A -| |–> B —-> C —-> D —-> Z(end product)
|__________________|
In the metabolic reaction shown above, it shows that substance A goes through a number of steps to turn into final product Z. This product will inhibit the reaction of A into B if built of which can be used to regulate the amount created which is basically known as Allosteric regulation. These type of reactions are usually regulated by Allosteric enzymes.

37
Q

What are a few properties of allosteric enzymes?

A
  • multi-subunit complexes
  • regulatory sites and catalytic sites are on different subunits
  • regulation occurs by confrontational changes
  • they dont use Michaelis-Menten kinetics
  • are used in feedback inhibitions in metabolic pathways.