enzyme kinetics Flashcards

1
Q

what is kinetics

A

study of reaction rates and how
they change in response to changes in
experimental parameters

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2
Q

name one key factor affecting rate of reaction

A

concentration [amount of substrate present]

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3
Q

when is Vo measured

A

@ start of reaction - little substrate has been converted -> product

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4
Q

Vo increases linearly with x but this rate slows down when?

A

an increase in the substrate - when more of the enzyme is used up until enzyme= saturated and is working @ its max. capacity # Vmax

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5
Q

what is Km

A

Michaelis-menten constant- the required substrate for enzyme to reach half Vmax

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6
Q

the lower the Km the…

A

tighter the substrate binds -> the enzyme// high affinity for substrate

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7
Q

enzyme inhibition is the goal of the pharmaceutical industry - give an e.g.

A

Aspirin inhibits cyclooxygenase, stops prostaglandin
synthesis and inhibits pain.
b) Statins inhibit HMG-CoA reductase in liver (which
makes cholesterol) controls heart disease.
c) Taxol inhibits microtubule protein prevents mitosis
and inhibits cancer

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8
Q

when developing a drug how does kinetics come into play

A

the rate at which the drugs effects the reaction can be obtained

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9
Q

enzyme kinetics is the study on chemical reactions that are catalysed by enzyme with a focus on their -

A

reaction rates

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10
Q

3D Modeling is useful when?

A

looking @ interaction between inhibitor and enzyme active site- helps design new drugs

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11
Q

structural information can aid drug development by? x3

A
  1. Providing information on the enzyme active site and its dimensions
    2.The nature of amino acid groups in the active site participating in catalysis.
  2. The nature of groups at the active site participating in substrate binding.
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12
Q

how can it be determined if an enzyme has an inhibitions

A

examine enzyme reaction in the presence of the potential inhibitor

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13
Q

hat are the 3 types of inhibition

A

-competitive inhibition
-non-competitive inhibition
-un-competitive inhibition

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14
Q

what other factors effect rate of an enzyme reaction

A

1) pH, enzymes operate within a range of pH optima outside this range the
enzyme activity may fall off. This may be due primarily to the ionisation of
groups at the active site which participate in binding or catalysis.
2) Heat, Enzymes as with all proteins are held together by forces such as
hydrogen bonding which are liable to be broken by heat. Thus heat can
result in chain unfolding and denaturation

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15
Q

the initial reaction velocity Vo is equal to?

A

rate at which the enzyme substrate complex is broken down

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16
Q

Km =?

A

substrate concentration @ which reaction velocity = 1/2 max

17
Q

what are on the axis of the lineweaver-Burk plot

A

1/Vo - y-axis versus - 1/S- x-axis

18
Q

Hanes-Woolf Plot has what on the axis

A

S - Y-axis and S/Vo on x-axxis

19
Q

a high vmax means

A

quick rate of reaction

20
Q

a low Km fast enzyme concentration eg.

A

2 x 10^-6 mM [binds more tightly]

21
Q

a high Km slow enzyme e.g. concentration

A

2 x 10^-2 mM

22
Q

which types of drugs are more specific and which type pf drugs have the best inhibition

A

more specific - competitive inhibitors
uncompetitive drugs = best inhibition

23
Q

the higher the enzyme affinity for a drug effects concentration how

A

higher the affinity the lower the concentration that can be used - the lower the dosage the better

24
Q

binding affinity is determined by?

A

Km

25
Q

what general type of enzyme is EC2.7.1.2

A

glucokinase