Enzymes Flashcards

1
Q

Define Metabolism

A

the sum of the chemical reactions that take place within each cell of a living organism

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2
Q

State and define the 2 types of metabolic reactions

A

catabolic-reactions that break down large molecules

anabolic-reactions that build complex molecules from simple ones

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3
Q

Give an example of anabolic reactions

A

an example of catabolic reactions are the formation of tissues and organs.Different cell components are synthesised and assembled in cells,which then form tissues and organs

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4
Q

Give an example of catabolic reactions

A

Example:Digestion

large molecules produced by digestion make up smaller molecules such as starch

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5
Q

Define extracellular and intracellular enzymes

A

extracellular-enzymes that work outside the cell that made them
intracellular-enzymes that work inside the cell

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6
Q

Explain how catalase catalyses intracellular reactions

A

Catalase is involved in the breakdown of H2O2 into water and oxygen.Catalase ensures this catabolic reaction occurs quickly,preventing it from accumulating as its toxic.

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7
Q

Explain how amylase catalyses extracellular reactions

A

Digestion of starch

Amylase breaks down starch into maltose(disaccharide)
Amylase is produced by salivary glands and pancreas (into pancreatic juice).

Maltose broken down into glucose by maltase

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8
Q

Explain what the temperature coefficient is

A

It shows how much rate of reaction increases when temp is increased by 10°C.

Eg:
If Q10 is 2 the rate of reaction is doubled when temperature is increase by 10°C

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9
Q

Draw a graph showing the effect of temp on enzyme action

A

Graph showing a line increasing reaching an optimum and decreases sharp decrease

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10
Q

Explain how an enzyme changes when temperature is increased

A

Increasing temperature gives the molecules more kinetic energy
• This gives more successful collisions
• More enzyme / substrate complexes form
• Enzymes have an optimum temperature
• Above this the hydrogen bonds that hold the tertiary structure are affected
• The 3D shape changes and the active site is distorted
• The change in shape prevents the substrate from binding
• The effect of high temperature is known as denaturing
• This is irreversible

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11
Q

Explain how changing PH affects enzyme shape.

A

When PH is decreased there are more H+ ions present. This affects ionic bonding and h bonds

The H+ ions will interact with the polar parts of an enzyme (delta negative). This will change the tertiary structure of the enzyme and substrate will no longer fit.

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12
Q

Explain how changing the substrate concentration affects enzyme structure/action

A

As the enzyme substrate concentration increases the rate of enzyme action increases.

The more substrate molecules present, the more frequent successful collisions.

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13
Q

Draw and label a graph showing affect of PH and substrate conc.

A

PH-symmetrical increases reaches optimum and decreases.

Substrate concentration - graph increases gradually and platues

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14
Q

Define cofactor

A

A non-protein substance bound to an enzyme, helping it with its function

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15
Q

explain how enzymes speed up reactions and how activation energy is lowered

A

activation energy lowered when an enzyme substrate complex is formed.

rate of reaction speeds up when activation energy is lowered.

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16
Q

compare induced fit model with lock and key

A

similarities:

  • interaction between active site and substrate
  • bonds in substrate are weakened when a ESC formed,lowering activation energy

differences:
- as the substrate moves into the active site, it interacts with the active site and interferes with the bonds that hold the shape of the active site.

17
Q

Define prosthetic group.Give example

A

inorganic cofactors that are permanently bound to enzyme.

Example:Zn+ prosthetic group for carbonic anhydrase

18
Q

what is difference between cofactors and coenzymes

A

cofactors are inorganic and coenzymes are organic.

19
Q

Define cofactor

A

Substances that must be preset for enzyme to catalyse a reaction.

Don’t participate directly in reaction so aren’t used up,can be used repeatedly.

cofactors can be stored in the body to be recycled/reused again and again.

20
Q

Explain how competitive inhibitors work

A

molecule similar to the shape of substrate binds to active site,preventing binding of substrate and enzyme from catalysing reaction

they compete with the substrate to bind to the active site.