Module 2.4 Flashcards

Enzymes

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1
Q

Role of enzymes

A

Catalyse reaction without being used up
Lower activation energy

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2
Q

Catalase role

A

Catalyses the break down of hydrogen peroxide into water and oxygen
Intracellular

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3
Q

Amylase role

A

Catalyses the break down of starch into maltose
Extracellular

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4
Q

What is specificity

A

The shape of the active site of the enzyme is complimentary to the shape of the substrate it is highly specific so will only catalyse reaction with the particular substrate that fits into the active site

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5
Q

lock and key hypothesis

A

Substrate fits into active site as they are complimentary shapes
bind forming enzyme substrate complex
product leaves the active site

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6
Q

Induced fit hypothesis

A

When the substrate enter the enzyme it causes a slight change in the shape so the conformation to the substrate is more precise
this allows the substrate to bind more effectively to the active site
enzyme-substrate complex
The product is formed but it has a slightly different shape to the substrate so detaches from the active site

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7
Q

Order of product formation

A

substrate, enzyme-substrate complex, enzyme-product complex, product

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8
Q

How enzymes catalyse reactions

A

Lower the activation energy by bringing the substrate molecules close enough together to react without excessive heat

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9
Q

Effect of pH

A

H+ and OH- ions break ionic bonds and H bonds in the tertiary structure causing the enzyme to denature when not at optimum pH

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10
Q

Effect of temperature

A

Kinetic energy from heat breaks H bonds in the tertiary structure
Enzyme denatures when over kinetic energy
Below optimum temperature rate of reaction is slower as there is less movement from kinetic energy so less collisions to form ES complexes

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11
Q

Effect of enzyme concentration

A

Rate of reaction will increase as concentration increases until substrate is limiting factor when rate will level off as all substrate molecules will have been turned into their product

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12
Q

Effect of substrate concentration

A

Rate of reaction will increase as concentration increases until enzyme is limiting factor when rate will level off as all enzyme active sites will be occupied

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13
Q

temperature coefficient (Q10) equation

A

rate of reaction at (T+10 degrees) / Rate of reaction at T degrees

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14
Q

What are coenzymes

A

small organic non-protein molecules that bind temporarily to the active site just before or at the same time as the substrate
They are chemically changed in the reaction

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15
Q

What are cofactors

A

small non-protein molecules that some enzymes need to work

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16
Q

What is the cofactor for amylase

A

Chloride ion

17
Q

Source of coenzymes

A

vitamins

18
Q

What is a competitive inhibitor

A

Similar shape to substrate
Fits into the active site so substrate cannot enter
Amount of inhibition depends on relative concentration of substrate and inhibitor
The active site is not changes
Reduces the number of free enzymes

19
Q

What is a non-competitive inhibitor

A

Binds to the allosteric site of the enzyme
Disrupts the tertiary structure and changes the enzymes shape
Active site shape changes
active site is no longer complimentary to the substrate ES complexes cannot form
Increasing substrate concentration will not impact the rate of reaction it will remain at a lowered level

20
Q

What is a prosthetic group

A

Type of cofactor
Permanently bound to an enzyme by covalent bonds

21
Q

What is a co-substrate

A

Type of cofactor joins with substrate to form correct shape to bind to active site

22
Q

What is end product inhibition

A

After a reaction has been catalysed product molecules stay bound to the enzyme so no more product can form