Chapter 4: Enzymes Flashcards

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1
Q

What is an enzyme?

A

Biological protein. Globular proteins that interact with substrate molecules causing them to react. Without them we would die

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2
Q

What is an anabolic enzyme?

A

Building up of molecules from smaller ones to larger ones

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3
Q

What is a catabolic enzyme?

A

The breaking down of molecules from larger ones to smaller ones. Eg: Digestion

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4
Q

Factors that affect enzyme activity?

A

Temperature, pH, concentration, pressure

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5
Q

What is activation energy?

A

The minimum amount of energy needed to start a reaction

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6
Q

Describe the Lock and Key model?

A

Enzyme has a tertiary structure with a complementary shape to a specific substrate molecule. This is called the active site. When substrate binds it’s called the enzyme-substrate complex then it reacts and forms the enzyme-product complex. The products then get released. There R-groups within the active site of the enzyme interact with substrate and form temporary bonds

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7
Q

Explain the induced-fit hypothesis?

A

When an enzyme’s active site actually changes shape slightly as the substrate enters. Initial reaction between enzyme and substrate is relatively weak but then the interactions rapidly induce changes in the tertiary structure and strengthen. It lowers the activation energy

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8
Q

What is an intracellular enzyme and examples?

A

An enzyme that acts within cells. The enzyme catalase ensures hydrogen peroxide is broken down into oxygen and water, preventing accumulation. IN animals and plants

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9
Q

What is an extracellular enzyme example

A

Enzymes outside of cells that break larger molecules into smaller ones.

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10
Q

How do single-celled organisms receive nutrients?

A

They release enzymes into the immediate environment and break down larger molecules such as proteins into amino acids and glucose to be absorbed into bloodstream

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11
Q

How is starch digested?

A

Starch polymers are broken down into maltose with the enzyme amylase. Produced in the salivary gland. Maltose is then broken down into glucose. With the enzyme maltase.

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12
Q

How are proteins digested?

A

Trypsin is a protease. A type of enzyme that catalyses the digestion of proteins into smaller peptides which is then broken down into amino acids. Trypsin is produced in the small intestine

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13
Q

What does Q10 equal and mean?

A

For every 10 degrees the temperature increases the rate of reaction doubles

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14
Q

How does temperature affect enzyme activity?

A

It increases the kinetic energy of the particles.Causes the particles to have more frequent successful collisions. Leads to an increase in rate of reaction

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15
Q

What is optimum temperature?

A

The temperature at which the enzyme has the highest rate of activity. Animals tend to have an optimum of 40 degrees

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16
Q

What happens if the enzyme temperature is too high?

A

Bonds holding the proteins break due to vibration. The breaking of the bonds causes the shape to change which means it has denatured

17
Q

What happens to enzymes in extreme temperatures?

A

Cells adapt to extremely cold or hot temperatures. Enzymes adapted to the cold have flexible structures making them less stable. Thermophiles (hot temp enzymes) are more stable and have hydrogen and sulphur bridges to strengthen bonds

18
Q

How does pH affect enzyme reactions?

A

A change in pH refers to a change in hydrogen ion concentration. The active site will only be in the right shape at certain hydrogen concentration. If the pH goes above optimum then the active site alters shape

19
Q

What happens to the enzyme physically with too much pH?

A

Structure is irreversibly altered. Active site is no longer complementary. Hydrogen ions interact with polar and charged R-groups. The more hydrogen ions present the less R-groups are available to interact so so bonds break.

20
Q

What happens if higher substrate concentration?

A

Increased number of substrate particles leads to higher collision rate with the active site and the enzyme making more enzyme-substrate complexes.

21
Q

What happens if higher enzyme concentration?

A

This increases the number of available active sites in a particular area leading to the formation of enzyme-substrate complexes at a faster rate

22
Q

What is an inhibitor?

A

Molecules that prevent enzymes from carrying out the normal function of a catalysis. Two types competitive and non-competitive

23
Q

How do competitive inhibitors work?

A

A molecule that has a similar shape to the substrate and can fit in the active site of an enzyme. This blocks the substrate from entering the active site preventing the enzyme from catalysing the reaction.

24
Q

What is a prosthetic group?

A

A cofactor that permanently bind to enzyme protein in order to activate them

25
Q

What does zinc do as a prosthetic group?

A

Inorganic and important part of the structure carbonic anhydrase and necessary for the metabolism of carbon dioxide

26
Q

what is an organic cofactor called?

A

A coenzyme

27
Q

What do coenzymes do?

A

Temporarily bind to enzyme active site and make it more complementary for the substrate

28
Q

How are inorganic cofactors obtained?

A

A mineral diet, for example: iron, calcium and chloride

29
Q

What is an inactive enzyme called?

A

Apoenzyme and an active one is holoenzyme

30
Q

What is end product inhibition?

A

Occurs when the product of an enzyme reacts as an an inhibitor in the enzyme that produces it. A negative feedback system. ATP is an example of this

31
Q
A