Enzymes Flashcards

1
Q

Are enzymes globular or fibrous?

A

Globular

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2
Q

What two things can enzymes affect in an organism?

A

Structure
Function

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3
Q

What is intracellular enzyme and example?

A

Works inside cells
Catalase- hydrogen peroxide breakdown catalysed

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4
Q

Extra cellular enzymes and example?

A

Work outside of cells
Amylase- catalyses hydrolysis of starch into maltose

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5
Q

What is an enzyme substrate complex?

A

A substrate bonded to an active site

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6
Q

What is an enzyme product complex?

A

Formed after reaction is catalysed, when product molecule is released from complex

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7
Q

Two models for enzyme action and explanation?

A

Lock and key- active site and substrate complementary in shape
Induced fit- active site undergoes conformational change after substrate binds, completing the fit

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8
Q

Two models for enzyme action and explanation?

A

Lock and key- active site and substrate complementary in shape
Induced fit- active site undergoes conformational change after substrate binds, completing the fit

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9
Q

How do enzymes speed up reactions?

A

By reducing activation energy

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10
Q

How does temperature affect rate of reaction at first?

A

Enzyme and substrate gain kinetic energy
More collisions and more enzyme- substrate complexes form
Rate of reaction increases to optimum temperature

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11
Q

How does temperature affect rate of reaction after optimum temperature?

A

-Molecules in enzyme begin to vibrate more
-Bonds in tertiary structure (ionic/hydrogen) break
-active site changes shape, no longer complementary to substrate
-enzyme denatures

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12
Q

What is the temperature coefficient (Q10)?

A

Unit-less value
Which indicates how much reaction changes if the temperature is increased by 10•C

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13
Q

Equation for temperature coefficient?

A

Q10= R2/R1
R2- rate at higher temp
R1- rate at lower temp

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14
Q

How do low pH’s affect rate of reaction?

A

H+ ions cause hydrogen and ionic bonds in tertiary structure in enzyme to break

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15
Q

How do high pH’s affect rate of reaction?

A

Presence of OH- causes ionic and hydrogen bonds in tertiary structure of enzyme to break

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16
Q

What is H+ and OH- ions overall affect on enzymes?

A

Enzyme may denature, shape of active site changes

17
Q

What does increasing enzyme concentration have on rate of reaction?

A

More successful collision
More enzymes substrate complexes form
Rate or reaction increase s

18
Q

Why does rate of reaction plateau when enzyme concentration increases?

A

Amount of substrate is limited, so adding more enzymes has no affect

19
Q

What effect does increasing substrate concentration have on rate of reaction?

A

More successful collision with active site
Rate increases
More enzyme-substrate complexes form

20
Q

Why does rate of reaction plateau when substrate is increased?

A

All available active sites are occupied

21
Q

What is Vmax?

A

Maximum rate of reaction

22
Q

What are inhibitors and what are the two types?

A

Molecules which bind to enzyme to reduce their activity
Competitive and non competitive inhibitors

23
Q

What do competitive inhibitors do?

A

Similar shape to substrate
Bind reversible to active site and block it, preventing substrate binding

24
Q

What affect does substrate concentration have on rate of reaction, when competitive inhibitors are involved?

A

-Increasing substrate concentration, increases rate of reaction
-As substrate concentration increases, there is a higher chance of substrate colliding with active site, instead of inhibitor molecule

25
Q

How do non competitive inhibitors work?

A

-They bind to allosteric site
-This causes active site to change shape, substrate can no longer bind

26
Q

What affect does increasing substrate concentration have on rate of reaction, when non competitive inhibitor is involved?

A

Little effect, as inhibitor and substrate do not compete
Vmax is dependant on inhibitor concentration

27
Q

For each type of inhibition, do the molecules bind reversible or irreversibly?

A

Both bind irreversibly and reversibly

28
Q

For each type of inhibition, do the molecules bind reversible or irreversibly?

A

Both bind irreversibly and reversibly

29
Q

What is a metabolic pathway?

A

Sequence of enzyme controlled reactions, where the product of one reaction, is reactant for next

30
Q

What is end product inhibition?

A

Final product of metabolic pathway acts as a reversible non competitive inhibitor for first enzyme

31
Q

What is the use of end product inhibition?

A

Regulates pathway, preventing build up of final product
When the levels of product start to fall, the inhibition levels decrease

32
Q

What are co factors and co enzymes?

A

Non protein molecules, which bind to enzymes, allowing them to function

33
Q

What are inorganic co factors?
Example?

A

Ions which bind to active site alongside substrate
They are not involved in reaction
Cl- ions are cofactors for amylase

34
Q

What are co enzymes?
Example?

A

-Organic molecules, bind alongside substrate
They are involved in the reaction, and are changed by it
-NAD removes H from ethanol via ethanol dehydrogenase

35
Q

Where are co enzymes sourced from?

A

Vitamins e.g. NAD comes from vitamin B3