Enzymes & Biochemical Pathways (4.1) Flashcards

1
Q

State the two major characteristics of enzymes

A
  1. Specificity

2. Catalytic Power

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2
Q

Describe enzyme specificity

A

Different enzymes act as catalysts for specific biochemical reactions by binding to specific substrate.

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3
Q

Some enzymes are able to act on multiple substrates. State whether this is true/false.

A

True. Enzymes can act on multiple substrates and catalyse multiple reactions.

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4
Q

Define substrate

A

Molecule which an enzyme acts upon

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5
Q

State whether or not enzymes are consumed when they catalyse reactions

A

No. Enzymes are not consumed when catalysing reactions.

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6
Q

Define catalytic power

A

Potential of an enzyme to increase the rate of a biochemical reaction

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7
Q

Describe what forms the enzyme active site

A

Tertiary protein folding

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8
Q

Describe the active site

A

Complex 3D shape that interacts with a specific substrate to catalyse specific reaction/s.

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9
Q

State what forms when the active site binds to the substrate

A

Enzyme-substrate complex

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10
Q

State the 2 enzyme-substrate interaction models

A
  1. Lock and key

2. Induced fit

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11
Q

State what stabilises the presence of the substrate in the active site

A
  • hydrogen bonds

- hydrophobic interactions

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12
Q

Describe the lock and key model

A

The active site and substrate fit as a lock and key

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13
Q

State the real-life object represented by the ‘lock’ in the lock and key model

A

The active site

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14
Q

State the real-life object represented by the ‘key’ in the lock and key model

A

The substrate

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15
Q

Describe the induced fit model

A

When a substrate binds to the active site of an enzyme, a conformational change occurs.

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16
Q

Describe conformational change

A

A change in the 3D arrangement of atoms in a macromolecule (e.g. protein or nucleic acid).

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17
Q

State whether or not some reactions can be catalysed in both directions

A

True. Some reactions can be catalysed in both directions

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18
Q

Describe activation energy

A

The energy that is required to start a biochemical reaction

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19
Q

Describe where the catalytic power of enzymes comes from

A

Ability to reduce activation energy

20
Q

Describe 3 ways that enzymes reduce activation energy

A
  1. proximity and orientiation
  2. micro-environment
  3. ion exchange
21
Q

Describe the effect of enzymes on proximity and orientiation

A

Enzymes bring reactants closer to one another to increase collision potential.

22
Q

Describe the effect of enzymes on the micro-environment

A

Reaction environment becomes non-polar to allow stabilising interactions to occur

23
Q

Provide 3 examples of stabilising interactions which occur in non-polar environment

A
  1. hydrogen bonding
  2. hydrophobic interactions
  3. van der Waals interactions
24
Q

Describe the effect of enzymes on ion exchange

A

Amino acids in the active site can often exchange H+ ions with the substrate.

25
State the 3 major types of biochemical pathways
1. linear 2. branched 3. cycles
26
Describe metabolism
Collection of all of the biochemical reactions that occur in living cells.
27
State the 2 major types of metabolic reactions
1. catabolic | 2. anabolic
28
Describe catabolic reactions
Reactions in which the substrates are broken down and energy is released
29
State whether catabolic reactions are exergonic or endergonic
Exergonic, because they release energy to break bonds between molecules.
30
Describe anabolic reactions
Reactions that require an input of energy in order to produce larger molecules from smaller substrates.
31
State whether anabolic reactions are exergonic or endergonic
Endergonic, because they require energy to form bonds between molecules.
32
Describe reaction coupling
A reaction that releases energy will be coupled with a reaction that requires an input of energy
33
State the 2 directions of biochemical reactions
substrate -> product | product -> substrate
34
Describe the structure of most enzymes
Globular | Tertiary or quaternary folding
35
Describe enzyme catalysis
Reactions are reversible and can be catalysed in both directions
36
Provide an example of an anabolic reaction
Building glucose in photosynthesis
37
Provide an example of a catabolic reaction
Breakdown of glucose in cellular respiration
38
Describe what activation energy is abbreviated as
E,A
39
Describe transition state
High-energy state which peaks after the desired activation energy has been added. Bonds must be broken in a reaction. For them to be broken molecules must be contorted to an unstable state
40
State the common form of activation energy
Heat
41
Describe the effect of heat on the behaviour of enzymes and substrates within a reaction
Thermal energy speeds up motion of reactants, increasing force and frequency of collisions allowing for bond breakage.
42
Describe the general trend between activation energy and reaction rate
The higher the activation energy the slower the reaction rate
43
Describe what the process of speeding up a reaction by reducing reaction rate is known as
catalysis
44
Describe what the factor that is added to reduce activation energy is known as
catalyst
45
Describe biological catalysts
enzymes