Enzymes Flashcards

1
Q

What are enzymes?

A

Types of proteins that are biological catalysts that speed up the rate of a reaction and are not used up in the reaction. Each enzyme is specific in its action.

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2
Q

What are enzymes made up of?

A

Most are made out of proteins, which are long chains of amino acids, and are held by hydrogen bonds to keep their 3D shape.

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3
Q

What do enzymes do?

A

They catalyse chemical reactions to make the reaction easier to take place, and are not used up in the reaction.
They are fast acting as they have a high turnover number number, which means they can convert many molecules of substrates per unit time.

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4
Q

What are the three parts of an enzyme reaction?

A

Substrate

Active site

Enzyme

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5
Q

What is a catabolic enzyme reaction?

🐱 🚗☄

A

Breaking a larger molecule into smaller parts. H2O is used in the reaction

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6
Q

What is an anabolic enzyme reaction?

A

Joining 2 or more substrate molecules together into a larger more complex one.

H2O is released in the process

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7
Q

How do enzymes help with the reaction?

A

They reduce the stability of bonds in reactants to speed up the reaction rate as enzymes reduce the input of energy required by lowering the activation energy needed for a reaction to take place, giving an alternative pathway.

Allow the reaction to take place at lower temps found in cells of organisms.

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8
Q

What is the activation energy?

A

The energy needed to start a chemical reaction

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9
Q

Explain the lock and key enzyme action process

🔐

A

The enzyme and substrate attach to each other like a lock and keys, as substrate fits into a specific active site of the enzymes to form the enzyme-substrate complex.

The products have a different shape after the reaction has occurred and so longer fits into the active site anymore and so are repelled.

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10
Q

Explain the induced fit enzyme action process.

A

Active site may not correspond to the shape of the substrate and so it is able to modify itself around the substrate as it is flexible.
As a result of these stresses on the substrate, the activation energy required to kick-start the reaction is dramatically lowered and new products are formed faster, and then are repelled.

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11
Q

How does the induced fit affect the reactant?

A

As a result of these stresses on the substrate, the activation energy required to kick-start the reaction is dramatically lowered and new products are formed faster.

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12
Q

What are four factors that affect the function of enzymes?

A

Temperature
pH levels
Concentration of substrate
Concentration of enzymes

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13
Q

How does temperature affect the function of enzymes?

A

Enzymes have a narrow temperature range and an optimal range where they operate the best at.

Increasing the temperature gives the molecules greater kinetic energy, thus increasing the rate of collision.

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14
Q

What if the temperature is increased to high?

A

If the temperature is increased, relative activity is increased, but if it is too high beyond its optimum, it can change the shape of the enzyme (denaturation), because of this the substrate will not be able to fit in, and so the enzyme will not be able to function anymore.

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15
Q

How does the high temperature cause denaturation?

A

As high temps break hydrogen bonds that hold enzymes together

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16
Q

What happens if the temperature is too cold?

A

It will cause the enzyme to stop operating as there is a reduction in particle movement and this will decrease the rate of reaction.

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17
Q

How does pH affect the function of enzymes?

A

Enzymes are sensitive to pH.
All enzymes have an optimum pH where their activity rate is the fastest, but if the pH is outside this range activity is reduced, and if it is really extreme (further away from its optimum) results in denaturation.

Different Enzymes function at different pH, Most have their optimum pH at 7

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18
Q

How does enzyme concentration affect the function of enzymes?

A

As if there is more enzymes added there will be more frequent collisions with substrates, making the reaction rate faster.

If there were less enzymes added then there be less frequent collisions with substrates, slowing down the reaction rate.

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19
Q

How does substrate concentration affect enzyme function?

A

As more substrates are added there will be more frequent collisions with enzymes and all of the active sites are filled, causing the reaction rate to go faster

At a low substrate concentration there will less frequent collisions with enzymes and not all of the enzyme active sites will be filled, causing the reaction rate to slow down.

20
Q

What if there is too much substrate is added?

A

If there is any further increase in substrate concentration, it will produce no significant change to the reaction rate as all the active sites of the enzymes will be saturated with a substrate

21
Q

What happens if you increase the concentration of substrates if a competitive inhibitor is present?

A

It can reduce the effects of a competitive inhibitor, as the inhibitor binding is reversible and so if there is more substrate present there is a greater chance of the substrate occupying the active site.

22
Q

What is the chemical structure of an enzyme?

A

They are globular proteins, amino acid chains that are folded and wound into a spherical shape.

23
Q

Why do extreme pH’s denature enzymes?

A

Acidity and alkalinity can affect the active site of enzymes. Free H+ (hydrogen ions) and OH- will affect the 3D shape of the enzyme and the active site.

24
Q

Why is only a small amount of enzymes needed to catalyse substrates?

A

As after the reaction takes place at the enzymes active site, the products are released and the active site is free to accept more substrates.

25
Q

What are cofactors?

A

Non-protein molecules that attach to enzymes to help it activate, it can increase the efficiency of the reaction, they also modifies the chemical structure of the enzyme in some way so that they can function more efficiently.

26
Q

What are cofactors made of?

A

Cofactors are small inorganic substances, such as Zinc ions and Magnesium ions

27
Q

What are the 3 types of cofactors?

A

Prosthetic groups
Coenzymes
Activators

28
Q

What are the prosthetic groups? (Cofactors)

A

Organic molecules that are not proteins that form a permanent attachment to the enzyme.

Eg. Organic: vitamins, sugar or lipid
Inorganic: metal ions

29
Q

What are coenzymes? (Cofactor)

A

Not permanently attached to the enzyme and are made of non-protein organic substances. They are made by organisms from dietary vitamins and act as carriers of substances to and from reactions that are catalysed by enzymes.

30
Q

What is an activator? (Cofactor)

A

Inorganic metal ions that form a temporary attachment to the enzyme and change its active site so the reaction is most likely to take place. Most activators are obtained from our diet.
Eg. Fe+, Mg2+ etc…

31
Q

What are inhibitors?

A

Substances that can attach to an enzyme and can slow down or stop a reaction

33
Q

What are the two types of inhibitors?

A

Reversible and Irreversible

35
Q

Explain non-competitive reversible inhibitors

A

They attach onto enzyme anywhere besides the active site. It alters the shape of the enzyme molecule, including the active site this prevents the enzyme from functioning correctly as the substrate can longer bind to the active site, reducing or stopping the reaction rate.

36
Q

Explain competitive reversible inhibitors

A

They have a similar structure to the substrate, so it competes with the substrate for the active site of an enzyme.
They lock onto the active site, therefore taking up the substrates spot and so the substrate is unable to fit in.
This prevents the formation of the enzyme-substrate complex and the rate of reaction decreases.

36
Q

What are Reversible inhibitors?

A

Temporarily effects the enzyme and when it is removed the enzyme regains its full activity.

36
Q

What are the two types of reversible inhibitors?

A

Competitive inhibitors

Non-competitive inhibitors

37
Q

What happens if you increase the concentration of substrate if a non-competitive inhibitor is present?

A

Increasing the amount of substrate will not reduce the inhibition as the shape of the enzyme is changed and so no substrates will be able to fit.

38
Q

What are non-reversible inhibitors?

A

Alter the enzyme permanently
Heavy metal ions such as Silver ions and mercury ions cause the Hydrogen bonds holding the enzyme together to break and so it loses its catalytic structure.

Eg. Cyanide is a non-reversible inhibitor of cytochrome oxidase, an important enzyme in respiration.

39
Q

What is cellular metabolism?

A

Sum of thousands of chemical reactions that occur constantly in each living cell

40
Q

What are biochemical pathways?

A

Chemical reactions in cells that occur in a series of enzymes regulated steps

41
Q

What are exergonic reaction?

A

Catabolic reaction, that is a downhill reaction.

When molecular bonds are broken to smaller molecules, a large amount of energy is released.

42
Q

What are endergonic reaction?

A

Anabolic reaction that is an uphill reaction.

It uses energy released by catabolic reactions to fuel anabolic reactions.

43
Q

What happens to the relative activity of the enzyme as pH increases?

A

As pH increases there is a corresponding increase in enzyme activity up to its optimum pH. Beyond this point enzyme activity decreases.

44
Q

Why are enzymes so vital for all living things?

A

enzymes control biochemical reactions in cells

If there were no enzymes to do such, no reactions would take place, therefore no energy available and the cell would cease to function

45
Q

Why would adding heat to supply activation energy be inappropriate for reactions that take place in cells?

A

May damage cells / denature enzymes