Enzymes Flashcards

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1
Q

What’s a catalyst?

A

Chemical that speeds up the rate of reaction and remains unchanged and reusable at the end of the reaction

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2
Q

What’s extracellular?

A

Outside the cell

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3
Q

What’s intracellular?

A

Inside the cell

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4
Q

What is metabolism

A

The chemical reactions that take place inside living cells or organisms

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5
Q

What’s a product?

A

Molecule produced from the substrate, by an enzyme catalyses reaction

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6
Q

What’s a substrate?

A

A molecule that is altered by an enzyme catalyses reaction

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7
Q

What are enzymes and what do they do?

A

Biological catalysts that speed up metabolic reactions in living organisms
Catalysts
Number of relations an enzyme catalyses per second is turnover number

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8
Q

What metabolic pathways are described as catabolic?

A

Where metabolites are broken down to smaller molecules and release energy

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9
Q

What metabolic pathways are described as anabolic?

A

Energy is used to synthesise larger molecules from smaller ones

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10
Q

What’s an active site?

A

Indented area on the surface of an enzyme molecule, with a shape that is complementary to the shape of the substrate molecule

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11
Q

What’s a cofactors?

A

A substance that has to be present to ensure an enzyme catalyses reaction takes place at the appropriate rate

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12
Q

What’s an enzyme substrate complex?

A

Complex formed by temporary binding of enzyme and substrate molecules during an enzyme catalyses reaction

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13
Q

What’s a prosthetic group?

A

A cofactors that is permanently bound by covalent bonds to an enzyme molecule

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14
Q

Describe carbonic anhydride and its function

A

Contain a zinc ion prosthetic group permanently bound to its active site
Found in erythrocytes
Catalyses conversion of carbon dioxide and water to carbonic acid which then breaks down into protons and hydrogen carbonate ions

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15
Q

How do unbound cofactors work?

A

Temporarily bind to enzyme or substrate to ease the formation of the complex therefore increasing rate of reaction
Some act as co substrates. The substrate and ion form correct shape to bind to active site
Some change charge distribution on the surface of substrate or active site and make the temporary complex bonds easier to form

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16
Q

What are coenzymes?

A

Small organic non-protein molecules that bind temporarily to the active site of enzyme molecules. They are chemically changed during the reaction and need to be recycled

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17
Q

What are enzyme product and enzyme substrate complexes?

A

An enzyme molecule with the products in its active site. Joined by non covalent force

Same with subtract instead of product

18
Q

What is Q10

A

Temperature coefficient

Calculated by dividing the t+10 by t

19
Q

Why do enzymes denature at high temperatures?

A

As temperature increases the enzymes vibrate more. This can break weak bonds in the tertiary structure such as hydrogen and ionic bonds.
This will cause the active site to change shape so the substrate will not fit into it.
This is irreversible
The enzymes are denatured

20
Q

What is a buffer?

A

Something that resists changes in pH

It can donate or accept hydrogen ions

21
Q

How does pH effect enzymes?

A

Excess proton interfere with hydrogen bonds and ionic forces so the active site changes shape. It also alters the charges on the active site as they cluster around negatively charged group

22
Q

How does pH affect rate of reaction?

A

Small changes reduce rate
Hydrogen bonds can reform if optimum pH is reached
Change can also be permanent if extreme pHs

23
Q

What is concentration?

A

Number of molecules per unit volume

24
Q

What’s an inhibitor?

A

Substance that stops or reduces a reaction

25
Q

What’s a competitive inhibitor?

A

Inhibition of enzyme. Similar shape to substrate and competes for active site. Prevents enzyme substrate complex

26
Q

What’s a non competitive enzyme?

A

Inhibition of enzyme. Attaches to part other than enzymes active site. Changes the shape of active site. Shape no longer complements substrate

27
Q

What can reduce competitive inhibition?

A

Increase substrate concentration

28
Q

What’s a competitor inhibitor the bonds irreversibly?

A

Inactivator

29
Q

Where to non competing enzymes bind?

A

Allosteric site

30
Q

How do non competitive inhibitors work

A

Distrupts the enzymes tertiary structure and changes it shape
Distortion changes shape of active site

31
Q

How can an enzyme catalyses reaction be regulated?

A

Negative feedback. Last product is a non competing inhibitor for 1st enzyme in metabolic pathway. This is reversible so can be detached when more product is required

32
Q

What do multi enzyme complexes do?

A

Increase efficiency of metabolic reactions without increasing substrate concentration
Keep substrates and enzymes in the same vicinity and reduce diffusion time.

33
Q

What’s an inhibitor?

A

Substance that stops or reduces a reaction

34
Q

What’s a competitive inhibitor?

A

Inhibition of enzyme. Similar shape to substrate and competes for active site. Prevents enzyme substrate complex

35
Q

What’s a non competitive enzyme?

A

Inhibition of enzyme. Attaches to part other than enzymes active site. Changes the shape of active site. Shape no longer complements substrate

36
Q

What can reduce competitive inhibition?

A

Increase substrate concentration

37
Q

What’s a competitor inhibitor the bonds irreversibly?

A

Inactivator

38
Q

Where to non competing enzymes bind?

A

Allosteric site

39
Q

How do non competitive inhibitors work

A

Distrupts the enzymes tertiary structure and changes it shape
Distortion changes shape of active site

40
Q

How can an enzyme catalyses reaction be regulated?

A

Negative feedback. Last product is a non competing inhibitor for 1st enzyme in metabolic pathway. This is reversible so can be detached when more product is required

41
Q

What do multi enzyme complexes do?

A

Increase efficiency of metabolic reactions without increasing substrate concentration
Keep substrates and enzymes in the same vicinity and reduce diffusion time.