Biochemistry: Enzyme Kinetics Flashcards

1
Q

what changes can result in a major implications for disease in terms of enzymes

A

distribution, abundance, efficiency

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2
Q

what can enzymes be used for in the lab

A

to develop diagnostic tests and drugs

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3
Q

in terms of enzymes activity, what is V

A

the no. of moles of a substrate converted per second

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4
Q

in terms of enzymes activity, what is Vmax

A

the maximum rate of enzyme activity (at infinite [S])

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5
Q

in terms of enzymes activity what is, what is half Vmax

A

the half-maximal rate of enzyme activity

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6
Q

draw the equation showing enzyme activity

A

E + S -K+1-> ES -K+2-> E + P

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7
Q

how do you measure Vmax

A

measure the initial reaction velocity at a known [S] and then increase [S] recording the reaction rate

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8
Q

what is the Michaelis constant

A

Km - the [S] at which the rate 1/2Vmax

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9
Q

does reaction rate ever reach Vmax

A

no

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10
Q

how would you calculate Km and Vmax for a true result

A

convert the results onto a straight line graph

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11
Q

what does a low Km mean

A

little substrate is needed to ilicit a have Vmax response

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12
Q

what does a high Km mean

A

a lot of substrate is needed to ilicit a have Vmax response

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13
Q

give an example of a reaction with a low Km and why

A
  • energy production in RBCs

- maintains the reaction even if there is a low glucose conc.

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14
Q

give an example of a reaction with ah igh Km and why

A
  • Proline Hydoxylases, need O2 to regulate transcription factors
  • allows O2 sensitive O2 sensing over physiological O2 ranges
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15
Q

what disease can a loss of proline hydroxylase result in

A

Monge’s Disease +/- Von Hippel Lindaw Syndrome

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16
Q

what are the 2 types of reversible inhibition

A

competitive and non-competitive

17
Q

what type of inhibition can be irreversible

A

non-competitive

18
Q

what is irreversible non-competitive inhibition

A

inihibtion irreversible

- usually via fomration or breakage of covalent bonds in the active site

19
Q

what happens to Km and Vmax in competitive inhibition

A

Km varies Vmax doesnt

20
Q

what happend to Km and Vmax in non-competitive inhibition

A

Km stays the same, Vmax varied

21
Q

how does feedback inhibition work

A

end products of a reaction inhibits the rate-limiting enzymes of a reaction

22
Q

what type of enzymes dont follow Michaelis-Menten rules

A

allosteric

23
Q

what enzymes tend to use feedback inhibition as a form of control

A

allosteric

24
Q

allosteric enzymes

A

changes conformtaion when effector binds

25
Q

in allosteric enzymes and increase in [S] shows what type of curve

A

sigmoid

26
Q

what modulates allosteric enzyme kinetics

A

allosteric factors

- allosteric inhibitors and activators

27
Q

what type of enzymes show co-operativity

A

allosteric

28
Q

give an example of allosteric enzymes that show co-operativity

A
  • Hb binding to O2, +ve co-operativity

- controlled by CO2, 2,3-BPG, H+