enzymes Flashcards

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1
Q

describe/define enzymes

A

protein molecules which act as biological catalysts. they greatly increase the rate of a chemical reaction without themselves being changed at the end of reaction

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2
Q

how to enzymes help metabolic reactions?

A

they are enabled to proceed rapidly but at low temperatures

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3
Q

what are the properties of enzymes?

A
  1. are proteins
  2. have active sites with a specific shape where the reaction take place
  3. effective in small amounts
  4. remain chemically unaltered at end of reaction
  5. function by lowering activation energy required for reaction to occur
  6. high degree of specificity
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4
Q

what is meant by a high degree of specificity? why do enzymes have this?

A

enzymes can be specific to one type of substrate molecule or a group of substrates with similar shapes.
the specifity of an enzyme is due to conformation at active site

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5
Q

how can the activity of an ezyme be changed? what is its implication?

A

it can be changed by the presence of inhibitors and activators. this implies that the rate of product formation can be controlled according to needs of the cell

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6
Q

describe the general structure of an enzyme molecule

A
  • complex globular shape and are relatively large molecules
  • only the active site of the enzyme comes into direct contact with the substrate
  • the shape of active site is complementary to shape of substrate
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7
Q

define activation energy

A

the energy required to make substances react

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8
Q

describe the Lock-and-Key hypothesis

A
  1. active site has a specific shape, to which the substrate binds
  2. the substrate is the “key”, whose shape is complementary to the shape of enzyme active site, which is the “lock”
  3. ‼ the shape of substrate(s) is complementary and fits exactly into shape of active site to form the enzyme-substrate complex
  4. once reaction is completed, the products are no longer complementary in shape and hence do not fit into active site, and leave the active site.
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9
Q

describe the Induced Fit hypothesis

A
  1. some enzymes and their active sites are physically flexible
  2. ‼ the shape of substrate(s) is complementary and does not fit exactly into shape of active site
  3. binding of substrate to active site induces a small conformational change in the shape of enzyme
  4. the substrate fits more snugly into active site to form enzyme-substrate complex, allowing the enzyme to perform catalytic function more effectively
  5. once reaction is completed, the products are no longer complementary in shape and hence do not fit into active site, and leave the active site.
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10
Q

describe how enzymes work at molecular level

A
  1. collision between enzyme and substrate at correct orientation causes substrate to bind to enzyme at its active site to form a short-lived enzyme-substrate complex
  2. within the complex, the chances of reaction occuring is greatly increased
  3. the reaction hence occurs
  4. once the reaction completes, the products formed and the unchanged enzyme molecule are released
  5. the enzyme is then able to catalyse another reaction
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11
Q

explain what happens when enzyme denatures

A

the enzyme unfolds and the precise shape is lost, so the conformation of the active site changes.
substrate cannot bind to the active site as its conformation is no longer complementary to the shape of substrate, and so the frequency of effective collision between substrate and enzyme molecules will decrease
(this process is usually irreversible)

adapted from 2023 EOY paper

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12
Q

state the typical range of optimum temperatures for mammalian enzymes

A

30-40°C

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13
Q

state the effect of increase of temperature up till optimum temperature on enzymes

A

as temperature increases, the kinetic energy of the enzyme and substrate molecules increases
the frequency of effective collisions between enzyme and substrate molecules increases
more enzyme-substrate complexes are formed per unit time

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14
Q

state the effect of optimum temperature on enzymes

A

at optimum temperature, enzyme functions at its maximum rate
the kinetic energy of enzyme and substrate molecules is the most ideal, resulting in highest frequency of effective collisions between enzyme and substrate molecules,
most enzyme-substrate complexes are formed per unit time

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15
Q

state the effect of temperature beyond optimum on enzymes

A

excess heat disrupts the intramolecular bonds which stabilise the structures of the enzyme
the enzyme denatures
the enzyme unfolds and the precise shape is lost, so the conformation of the active site changes.
substrate cannot bind to the active site as its conformation is no longer complementary to the active site, and so the frequency of effective collision between substrate and enzyme molecules will decrease

same ending explanation as before

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16
Q

state the effect of freezing temperatures on enzymes

A

enzymes are inactivated
enzyme activity is low due to less kinetic energy
lower frequency of effective collision between substrate and enzyme molecules to form enzyme-substrate complexes

17
Q

describe the effect of optimum pH on enzymes

A

at optimum pH, enzyme functions at its maximum rate
the intramolecular bonds maintaining the protein structure of enzyme are intact
conformation of active site is most ideal for substrate binding
hence highest frequency of effective collision between enzyme and substrate molecules
greater number of enzyme substrate molecules formed per unit time

18
Q

describe the effect of pH higher or lower than optimum on enzymes

A

the H+ concentration changes
the intramolecular bonds maintaining the protein structure of enzyme are altered
the enzyme denatures
the enzyme unfolds and the precise shape is lost, so the conformation of the active site changes. substrate cannot bind to the active site as its conformation is no longer complementary to the active site, and so the frequency of effective collision between substrate and enzyme molecules will decrease

(within a certain range, this is reversible. at extreme pH changes, the conformation will be severely altered)

same ending explanation as before

19
Q

describe the effect of substrate concentration on enzymes

A

for a fixed enzyme concentration, rate of enzyme reaction increases with increasing substrate concentration
an increase in number of substrate molecules leads to an increase in frequency of effective collision between enzyme and substrate molecules
more enzyme-substrate complexes formed per unit time
rate of reaction increases
the rate of reaction is limited by substrate concentration.

there is a point where further increase in substrate concentration does not significantly change the rate of reaction
because all active sites of all enzyme molecules are saturated with substrate molecules
any free substrate molecules has to wait until enzyme-substrate complexes have released its products before it can enter the active site of enzyme itself
the rate of reaction is now limited by enzyme concentration.

20
Q

describe the effect of enzyme concentration on enzymes

A

for a fixed substrate concentration, rate of enzyme reaction increases with increasing enzyme concentration
an increase in number of enzyme molecules leads to an increase in frequency of effective collision between enzyme and substrate molecules
more enzyme-substrate complexes formed per unit time
rate of reaction increases
the rate of reaction is limited by enzyme concentration.

there is a point where further increase in enzyme concentration does not significantly change the rate of reaction
as the rate of reaction is now limited by enzyme concentration.

21
Q

sketch the graphs of the effects of:
1. temperature
2. pH
3. [substrate]
4. [enzyme]

A