Enzymes Flashcards

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1
Q

What type of molecules are enzymes?

A

Enzymes are globular proteins that act as biological catalysts.

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2
Q

Describe the structure of an enzyme.

A

Enzymes have a specific 3D structure with an active site formed by folded chains of amino acids held by hydrogen bonds, ionic bonds, and disulfide bridges.

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3
Q

Define the term complementary.

A

Complementary refers to the specific fit between the enzyme’s active site and its substrate, like a lock and key.

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4
Q

What do enzymes do?

A

Enzymes speed up biochemical reactions by lowering the activation energy required for the reaction.

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5
Q

What is meant by the term biological catalyst?

A

A biological catalyst is a substance, like an enzyme, that increases the rate of a chemical reaction in a living organism without being consumed.

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6
Q

Why are many different enzymes needed for different reactions?

A

Different enzymes are needed because each enzyme has a specific active site that only fits particular substrates.

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7
Q

How do enzymes lower activation energy?

A

Enzymes lower activation energy by binding to substrates at their active sites, forming an enzyme-substrate complex and stabilizing the transition state.

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8
Q

What is the difference between catabolic and anabolic enzymes?

A

Catabolic enzymes break down large molecules (e.g., amylase breaking down starch). Anabolic enzymes build larger molecules (e.g., DNA polymerase synthesizing DNA).

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9
Q

What is an enzyme-substrate complex?

A

An enzyme-substrate complex is the temporary structure formed when a substrate binds to the enzyme’s active site.

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10
Q

Describe the lock and key hypothesis.

A

The lock and key hypothesis states that the enzyme’s active site is a specific shape that perfectly fits the substrate, like a key fitting into a lock.

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11
Q

Describe the induced fit hypothesis.

A

The induced fit hypothesis suggests that the enzyme’s active site changes shape slightly to fit the substrate more snugly when it binds.

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12
Q

How do the lock and key hypothesis and the induced fit hypothesis differ?

A

The lock and key hypothesis suggests a rigid active site, while the induced fit hypothesis suggests a flexible active site that changes shape to fit the substrate.

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13
Q

What are the limitations of the lock and key hypothesis?

A

Limitations include not explaining enzyme flexibility, wide substrate interactions, and how enzymes lower activation energy by stabilizing the transition state.

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14
Q

What is the difference between intracellular and extracellular enzymes?

A

Intracellular enzymes function inside cells, while extracellular enzymes are secreted outside cells and function in external environments like digestion.

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15
Q

Name an intracellular enzyme and its function.

A

Catalase, which breaks down toxic hydrogen peroxide into water and oxygen inside cells.

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16
Q

Name an extracellular enzyme and its function.

A

Amylase, which breaks down starch into maltose in the digestive system.

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17
Q

what is the effect of substrate concentration on enzyme activity

A

the higher the substrate concentration, the more frequent collisions meaning a higher rate of reaction. This is only up until Vmax is reached when the enzymes become the limiting factor so no more reactions happen.

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18
Q

what is the effect of enzyme concentration on enzyme activity

A

the higher the enzyme concentration, the more frequent collisions meaning a higher rate of reaction. This is only up until Vmax is reached when the substrates become the limiting factor so no more reactions happen.

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19
Q

why does enzyme activity increase with temperature?

A

the heat gives the enzymes more kinetic energy so there are more frequent collisions between the active site of the enzyme and the substrate, increasing the rate of reaction

20
Q

what happens to enzyme activity when the temperature increases past the optimum?

A

the rate of reaction decreases because the enzymes become denatured as the hydrogen bonds between them start to break causing the tertiary structure of the enzyme to change. this change of the tertiary structure alters the active site so the enzymes can no longer bind to their substrate, making them denatured and non-functioning. Once an enzyme has denatured it can’t be renatured as the tertiary structure has been changed too much.

21
Q

what is the temperature coefficient (Q10)

A

ROR at temperature X + 10 degrees / ROR at temperature X

22
Q

what is pH?

A

how many hydrogen (H+) ions are present
low pH= high concentration of hydrogen ions

high pH= low concentration of H+

23
Q

what are the average optimum pH’s for intracellular and extracellular enzymes?

A

intracellular= 7.3 - 7.4
extracellular= function at different pH’s in the same organism

24
Q

how does pH effect enzyme activity?

A

large changes in pH disrupts the hydrogen and ionic bonds - disrupting the active site. Hydrogen ions interact with polar charged R groups. The more hydrogen ions present (low pH) the less R-groups are able to interact with each other so the bonds break and the shape of the enzyme changes. The reverse is true when fewer hydrogen ions are present. This means the shape of the active site will change as the pH changes and therefore it will only function within a narrow pH range

25
Q

What is an enzyme inhibitor?

A

An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity by either blocking the active site or altering its shape.

26
Q

What are the two main types of enzyme inhibition?

A

The two main types are competitive inhibition and non-competitive inhibition.

27
Q

How does competitive inhibition work?

A

In competitive inhibition, the inhibitor molecule resembles the substrate and competes for the active site, blocking the actual substrate from binding.

28
Q

How can competitive inhibition be overcome?

A

By increasing the concentration of substrate, which makes it more likely for the substrate to bind to the active site rather than the inhibitor.

29
Q

How does non-competitive inhibition work?

A

In non-competitive inhibition, the inhibitor binds to a site other than the active site (allosteric site), causing a change in enzyme shape that reduces its activity.

30
Q

Can non-competitive inhibition be overcome by increasing substrate concentration?

A

No, because the inhibitor affects enzyme function by altering its shape, not by competing with the substrate for the active site.

31
Q

What is an allosteric site?

A

An allosteric site is a location on an enzyme other than the active site where molecules (such as non-competitive inhibitors) can bind and alter enzyme activity.

32
Q

What effect does a competitive inhibitor have on the Vmax of an enzyme?

A

A competitive inhibitor does not change the Vmax of an enzyme, as maximum reaction rate can still be reached with enough substrate concentration.

33
Q

What effect does a non-competitive inhibitor have on Vmax?

A

Non-competitive inhibition decreases the Vmax because it reduces the number of active enzyme molecules available, regardless of substrate concentration.

34
Q

What is an irreversible inhibitor?

A

An irreversible inhibitor binds permanently to an enzyme, usually at the active site, permanently inactivating it.

35
Q

Give an example of an irreversible inhibitor and its action.

A

Cyanide is an example; it binds irreversibly to cytochrome c oxidase in the electron transport chain, blocking cellular respiration.

36
Q

How do drugs act as enzyme inhibitors?

A

Some drugs are enzyme inhibitors; for example, penicillin inhibits enzymes needed for bacterial cell wall synthesis, thereby killing bacteria.

37
Q

Why are enzyme inhibitors important in metabolic regulation?

A

Enzyme inhibitors can control reaction rates, prevent overproduction of products, and help regulate metabolic pathways by slowing or stopping specific reactions.

38
Q

What do many enzymes need to function properly?

A

Many enzymes function in partnership with another chemical called a cofactor.

39
Q

What are the substrates for the enzyme amylase and what additional component is required for amylase to catalyse reactions?

A

The substrates for amylase are starch and water.
The chloride ion must attach to the amylase molecule for the reaction to occur; without it, amylase cannot catalyse the reaction.

40
Q

In the context of amylase, what role does the chloride ion play and where do we obtain chloride ions?

A

The chloride ion acts as a cofactor for amylase, but it is not a substrate.
Chloride ions are obtained from our diet.

41
Q

What is NAD, and what is its role?

A

NAD is a large organic molecule that temporarily binds to enzymes involved in respiration, transferring hydrogen atoms from one molecule to another.

42
Q

What is the term used for large organic cofactors like NAD?

A

Large organic cofactors like NAD are called coenzymes

43
Q

Where do many coenzymes come from?

A

Many coenzymes come from vitamins in our diet.

44
Q

From which vitamin is NAD derived?

A

NAD is made from niacin, also known as vitamin B3.

45
Q

What is a prosthetic group and what is an example of a prosthetic group?

A

A prosthetic group is a cofactor that is a permanent part of the enzyme’s structure.
An example is the zinc ion in carbonic anhydrase, which is permanently bound to the enzyme.