Enzymes, Kinetics and Inhibition Flashcards

(34 cards)

1
Q

enzyme

A

is a biological catalyst

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2
Q

Biological

A

Most enzymes= globular proteins (mostly spherical and water soluble)

Can have Abzymes

other options:
Ribozymes
DNAzymes

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3
Q

Catalyst

A

Accelerates rate of reaction

Doesn’t get involved
> Wear out/ don’t last forever

Acts on some other molecule/substance

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4
Q

what are enzyme reactions

A

enzyme reactions are ‘specialised’ chemical reactions

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5
Q

chemical reactions

A

Reactants are converted into products.
May involve a catalyst.
Rate of reaction can be measured.
Rate increases as temperature increases essentially without limit.

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6
Q

Enzyme Reactions

A

Substrates are converted into products.
Always involves a catalyst (the enzyme).
Rate of reaction can be measured.
Rate increases as temperature increases up to a limit.

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7
Q

Active site

A

A particular region where the other molecule binds.

Has a 3D conformation.

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8
Q

Enzyme Kinetics

A

area of study involving measuring the rates of reaction of enzymes.

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9
Q

the catalytic rate constant

A

is the rate constant for the conversion of ES into EP

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10
Q

ES complex

A

can dissociate back into E and S without formation of P

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11
Q

Km

A

is the [S] which will give a velocity equal to half the Vmax

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12
Q

The Michaelis-Menten Equation

A

Allows us to calculate the expected velocity at a given [S] as we have established the Vmax and Km for an E/S reaction pair.

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13
Q

The Law of thermodynamics

A

> The rate of any chemical reaction is sensitive to temperature.
An increase in temperature leads to an increase in reaction rate.
A common rule of thumb is that a 10 degrees increase doubles the rate of a reaction.

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14
Q

what is pH ?

A

is a measure of acidity

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15
Q

what terminals do proteins contain?

A

N-terminal = NH3 group
C-terminal = COOH group

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16
Q

key effect of pH on enzyme activity is mediated by ….

A

changes in the charge state of amino acids involved in the catalytic reaction.

17
Q

active from of enzymes

A

only when the R1 side chain is pronated and the R2 is not.

18
Q

the pH optimum

A

the pH the enzyme works best at

19
Q

substrates can become ionised meaning

A

the overall charge on a substrate may influence which enzymes can act on it.

20
Q

examples of substrates that may be charged

A

Organic acids
Phosphate esters
Nucleotides

21
Q

why do we call enzymes inhibited ?

A

when the enzyme cannot complete a catalytic cycle.

22
Q

net effect =

A

= reduced conversion of S —> P

In kinetic terms:
The velocity of a reaction decreases
Reaction does proceed but not as quickly
Something gets in the way –> the inhibitor, I

23
Q

Reversible inhibition

A

Inhibitor can bind to and dissociate from the enzyme.

Activity is lost when inhibitor is bound.

Wait for enzyme to become free to overcome.

24
Q

Irreversible inhibition

A

Enzyme is covalently modified and activity lost.

Replace enzyme to overcome.

25
Reversible inhibition forms:
Competitive Uncompetitive Mixed
26
Competitive inhibition
Inhibitor binds at the active site. Prevents substrate binding.
27
Uncompetitive inhibition
Inhibitor binds to the EScomplex. Not at active site.
28
Mixed inhibition
The inhibitor can bind to the free enzyme or the EScomplex.
29
Aspirin
the classic suicide inhibitor Irreversibly inactivates an cyclooxygenase II Involved in prostaglandin synthesis.
30
!!!!!
At high [S] the excess P formed leads to inhibition.
31
what has roles to overcome activation energy
Proximity Distortion
32
!!!!
velocity of a reaction increases when [S] increases
33
!!!!!!!!
The Km is the [S] which will give 1/2Vmax
34
Enzyme inhibitors
block enzyme action