4.1-4 Enzymes Flashcards

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1
Q

What do enzymes do?

A
  • increase the rate of reaction by lowering the activation energy of the reaction they catalase
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2
Q

What is the active site?

A
  • the area of the enzyme where the reaction with the substrate takes place
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3
Q

What is enzymes relation to substrates?

A
  • enzymes are specific to substrates they bind to meaning that only one type of substrate fits into the active site of the enzyme
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4
Q

What happens when the enzyme and substrate form a complex?

A
  • the structure of the enzyme is altered so that the active site of the enzyme fits around the substrate
  • this is called the induced fit model
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5
Q

What are the four factors effecting the rate of enzyme controlled reactions?

A
  • enzyme concentration
  • enzyme pH
  • temperature
  • substrate concentration
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6
Q

How does enzyme concentration effect the rate of reaction?

A
  • the rate of reaction increases as enzyme concentration increases as there are more active sites for substrates to bind to
  • increasing enzyme concentration beyond a certain point has no effect on the rate of reaction as there are more active sites than substrates so substrate becomes the limiting factor
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7
Q

How does substrate concentration effect the rate of reaction?

A
  • as concentration of substrate increases, the rate of reaction increases as more enzyme-substrate complexes are formed
  • beyond a certain point the rate of reaction no longer increases as enzyme concentration becomes the limiting factor
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8
Q

How does temperature effect the rate of reaction?

A
  • rate of reaction increases up to the optimum temperature, which the temperature at which enzymes work at their maximum rate
  • rate of reaction decreases above the optimum temperature as enzymes can denature
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9
Q

What is an inhibitor?

A
  • a substance which slows down or stops a reaction by affecting the binding of substrate to enzymes
  • can be reversible or irreversible
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10
Q

Examples of irreversible inhibitors are …

A
  • heavy metal ions such as mercury and silver which cause disulphide bonds within the protein structure to break, as a result causing the shape of active site to change, thus affecting protein activity
  • cyanide which is nerve gas that covalently binds to the active site, therefore preventing the binding of the substrate
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11
Q

What in an reversible inhibitor?

A
  • bind to the active site through hydrogen bonds and weak ionic interactions therefore they do not bind permanently
  • can either be competitive or non-competitive
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12
Q

What are competitive inhibitors?

A
  • are similar in structure to the substrate molecule therefore they bind to the active site of the enzyme, decreasing its activity as they compete with substrate for the enzyme
  • the amount of product formed remains the same, however the rate at which product formation occurs decreases
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13
Q

What is the effects that occur in the change of concentration in the competitive inhibitors?

A
  • the high the concentration of competitive inhibitor the lower the reaction rate
  • increasing the substrate reverses the effect of competitive inhibitors by out-competing them
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14
Q

What are non-competitive inhibitors?

A
  • it binds at another site on the enzyme known as the allosteric site
  • binding of the non-competitive inhibitors changes the shape of the active site therefore preventing the binding of the substrate
  • increasing the concentration of substrate has no effect on non-competitive inhibition
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15
Q

Examples of inhibitors …

A
  • drugs
  • penicillin which is used to fight bacterial infections, it is an inhibitor of enzyme transpeptidase which plays an important role in cell wall formation
  • ritonavir which is an antiretroviral drug used to treat HIV which inhibits HIV protease which is responsible for assembly of new viral particles and spread of infection
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16
Q

What is a cofactor?

A
  • a non-protein compound required for the enzyme’s activity to occur
17
Q

What are the three types of cofactor?

A
  • coenzymes
  • activators
  • prosthetic groups
18
Q

What are coezymes?

A
  • organic cofactors which do not bind permanently
  • they facilitate the binding of substrate to enzyme
19
Q

Coezymes are vitamin deprived, what are examples of this?

A
  • NAD derived from niacin, which acts as a hydrogen acceptor
20
Q

What are activators?

A
  • inorganic metal ions which temporarily binds to the enzyme and alters its active site, making the reaction more feasible
21
Q

Example of activators is …

A
  • magnesium ions are important activator which is involved in processes such as shielding negative charge
22
Q

Where are prosthetic groups found?

A
  • are permanently attached to an enzyme
23
Q

Examples of prosthetic groups are …

A
  • haemoglobin contains a prosthetic haem group which contains iron, permanently bound to the molecule, which serves as a means of binding oxygen
24
Q

What is substrate concentration in the role of collisions?

A
  • once all of the enzymes active sites are full, adding more substrate won’t make much of a difference
25
Q

Why did the lock and key theory swap to the induced fit theory?

A
  • theories are moved by the more experimental theories
26
Q

Enzymes are proteins formed in the cell but work/ react differently. What are the two categories of this?

A

extracellular = work outside the cell
intracellular = work in the cell

27
Q

Two examples of intracellular reactions are …

A

lactase = breaks down lactose into glucose and galactose
catalase = breaks hydrogen peroxide down into water and oxygen

28
Q

Two examples of extracellular reactions are …

A

amylase and pepsin = work outside the cell in the human digestive system
amylase = is secreted by salivary glands, it catalyses the hydrolysis of starch into maltose

29
Q

What is product inhibition?

A
  • metabolic pathways are often a series of reactions
  • many enzymes are inhibited by the product of their reaction
  • end production inhibition is when the final product inhibits an enzyme acting earlier in the pathway