Session 2: Enzymes Flashcards

1
Q

What is the metabolic process of anabolism?

A

the formation of macromolecules (complex molecules) from monomers by condensation reactions.

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2
Q

What is the metabolic process of catabolism?

A

the breakdown/hydrolysis of macromolecules (complex) into monomers (simple molecules).

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3
Q

What is metabolism? Do anabolic reactions or catabolic reactions produce energy?

A

Chemical reaction in bodies cells, turn food into energy, metabolism requires enzymes. Anabolic reactions require energy in order to occur, catabolic reactions produce energy.

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4
Q

What are metabolic pathways?

A

Metabolic pathways are where enzymes work together, each enzyme is a step in a series of steps, in order for a metabolic reaction to occur. They are a series of linked biochemical reactions where enzymes activate each step of the pathway. Pathways are controlled by regulating the amount of enzyme present. (Product for one step becomes substrate for the next, etc.)

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5
Q

What is the lock & key theory of catalysing enzymes?

A

Substrate is the key, active site is the lock. There is one specific enzyme for one specific substrate.

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6
Q

What is the Induced Fit model/theory of catalysing enzymes?

A

Also known as broad specificity, Induced fit is where some enzymes will undergo conformational change after the substrate goes into the active site. The active site will physically change to fit the substrate more snugly. This theory means that enzymes can bind to multiple kinds of substrates.

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7
Q

How do enzymes speed up the rate of reaction?

A

Enzymes lower the amount of activation energy (Ea) (amount of energy required for a reaction to occur) because when an enzyme binds to a substrate it stresses and destabilises bonds in the substrate, increasing reactivity. With enzymes, reactions can occur faster and more efficiently.

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8
Q

What is a cofactor? And what are the three types of cofactors?

A

Some enzymes require non-protein cofactors to complete catalytic properties and functions. The three types of cofactors are inorganic ions, coenzymes, and prosthetic groups.

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9
Q

What are the four factors which impact enzymes?

A

Enzymes have their own individual sets of conditions in which they work best. The factors are enzyme concentration, substrate concentration, temperature, and acidity and alkalinity (pH).

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10
Q

What is enzyme inhibition?

A

Inactivation of an enzyme. Can be reversible or irreversible, competitive or non-competitive. It can occur at high temperatures or by changes in pH (non-specific factors that would inactivate any enzyme). Enzyme activity can also be regulated by specific factors, such as poisons because they bind to particular enzymes and inactivate them.

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11
Q

What is the difference between competitive and non-competitive inhibition?

A

Competitive inhibition is where the inhibitor tries to reach the active site before the substrate can (will have similar structure to substrate so it can fit). Competitive inhibition is generally reversible, it will leave the active site and the substrate goes in and the reaction continues as normal. Non-competitive inhibition is when the inhibitor binds to site other than the active site (allosteric site) and causes conformational change to the active site so that the substrate cannot fit. Non-competitive inhibition is generally irreversible (will stay permanently attached)

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12
Q

What is enzyme denaturation?

A

when chemical bonds are broken due to (changes) in temperature and pH outside the enzymes optimum range. Denatured enzymes are no longer active and cannot function.

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13
Q

What is an enzyme (revision)?

A

An enzyme is a biological catalyst that speeds up biological reactions and regulates cell metabolism. They bind to substrates at the active site.

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14
Q

What is an inorganic ion (cofactors)?

A

Examples include iron, magnesium, and zinc (ions have charge). Ions may help to stabilise structure of enzyme or may take part in the reaction at the active site.

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15
Q

What is an organic molecule/coenzyme (cofactors)?

A

These types of cofactors link different enzyme/catalysed reactions into a sequence during metabolic processes. They often accept or donate hydrogen ions or chemical groups. Vitamins are important in the production of coenzymes.

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16
Q

What is a prosthetic group (cofactors)?

A

They attach permanently to enzymes. Assist and are essential to proper enzyme function, help to form final 3D shape of the enzyme.

17
Q

Explain the cofactor equation.

A

A holoenzyme or active enzyme is reached when an apoenzyme or inactive protein component is added to a cofactor.

apoenzyme + cofactor = holoenzyme

18
Q

Explain the enzyme condition factor: substrate concentration. What does its graph look like?

A

Amount of substrates. rate of reaction will increase as substrate concentration increases (up to a point because active sites become saturated). It’s graph is increasing (almost linear) and then plateauing (point of saturation)

19
Q

Explain the enzyme condition factor: enzyme concentration. What does its graph look like?

A

If there is sufficient substrate present, rate of reaction will increase as enzyme concentration increases. It’s graph is linear (appears to be linear?)

20
Q

Explain the enzyme condition factor: temperature. What does its graph look like?

A

The correct temperature means the best rate of reaction where kinetic energy means the particles are moving faster = higher chance of collision. Denaturation of enzyme occurs after certain temperature (too hot). It’s graph is polynomial/a bell curve where the optimal temperature is at the top of the curve.

21
Q

Explain the enzyme condition factor: acidity and alkalinity (pH). What does its graph look like?

A

pH is much like temperature where each enzyme has a specific range in which it works, and significant change from the level can alter chemical bonds and cause denaturation. It’s graph is the same as temperature (a bell curve where the top of the curve is the optimum pH level).

22
Q

What is an enzyme inhibitor?

A

A molecule that disrupts a normal reaction pathway (causes enzyme inhibition). Can be competitive or non-competitive, they prevent the formation of enzyme-substrate complex and hence prevent formation of a product. Can be reversible or irreversible depending on specific effect of the inhibitor being used.

23
Q

What is end-product inhibition?

A

When the products of metabolism regulate metabolic pathways. The product of the process inhibits the enzyme in step one of the process, stopping the process. When you run out of product, it cannot stop step one anymore and the reaction continues until there’s enough product to stop the reaction again.

24
Q

What does maltase do?

A

breaks down maltose (into two alpha glucoses)

25
Q

What does sucrase do?

A

breaks down sucrose (into glucose and fructose)

26
Q

What does lactase do?

A

breaks down lactose (into galactose and glucose)

27
Q

What does lipase do?

A

breaks down lipids/fats into fatty acids

28
Q

What does amylase do?

A

breaks down amylose (part of starch - maltose and glucose)

29
Q

What does trypsin do?

A

breaks down proteins

30
Q

What does pepsin do?

A

breaks down proteins

31
Q

What does protease do?

A

breaks down proteins