Physiology and metabolism 1-7 Flashcards Preview

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Flashcards in Physiology and metabolism 1-7 Deck (35)
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1
Q

How do enzymes affect the chemical equilibrium

A

Enzymes have no effect as they increase the forward and backward reaction

2
Q

How is catalytic power expressed

A

The turnover number or catalytic constant (Kcat)

3
Q

Define Kcat

A

The number of molecules of substrate that one enzyme molecule can convert in 1 second

4
Q

What are co-factors

A

Small molecules not part of the enzyme but are required for activity. These can be metal ions or other organic molecules

5
Q

Enzymes classifications

A
  • Oxidoreductases
  • Transferases
  • Hydrolases
  • Lyases
  • Isomerases
  • Ligases
6
Q

What is the active site

A

Part of the enzyme in contact with the substrate. Many weak non-covalent interactions form between the substrate and active site.

7
Q

How is the active site formed

A

It is a 3-dimensional structure formed from the folding of the polypeptide chain.

8
Q

What is the lock and key model

A

Active sites were initially pictured as a fixed set of chemical groups exactly fitting the substrate.

9
Q

What is the induced fit model

A

Continuous change in the conformation and shape of the enzyme in response to substrate binding. Allows a greater degree of specificity as they also have to interact.

10
Q

What is a transition state

A

The highest energy state interval along the pathway from substrate to product.

11
Q

What is the activation barrier

A

The difference in energy between reactants and the transition state.

12
Q

How do enzymes speed up the rate of the reaction

A

They lower the activation barrier by providing an alternative pathway which stabilises the transition state.

13
Q

Another name for enzyme substrate complex

A

Michaelis complex

14
Q

What is a catalytic triad

A

A group of 3 amino acids found on the active site of some proteases involved in catalysis. They form part of the active site.

15
Q

Conditions needed for steady state kinetics

A

substrate&raquo_space; enzyme

16
Q

How to measure the rates of enzyme catalysed reactions

A
  • Measure appearance of product, or disappearance of substrate (keep pH and T constant)
  • In a continuous assay
  • Work in conditions where substrate&raquo_space; enzyme
17
Q

What is the michaelis-menten equation

A

V=Vmax.[s]/Km+[s] ,where Km is a measure of affinity

18
Q

How to find Km from a velocity substrate graph

A

substrate at 1/2 Vmax

19
Q

How to calculate enzyme efficiency

A

Kcat/Km

20
Q

What is the lineweaver-burk plot

A
  • Plot 1/v against 1/s
  • y intercept = 1/vmax
  • x intercept = -1/km
  • gradient = Km/Vmax
21
Q

What is an eadie-hofstee plot

A
  • A plot of V against V/S
  • Gradient = -Km
  • X intercept = Vmax/Km
  • Y intercept = Vmax
22
Q

What are thermophiles

A

Enzymes that retain activity at high temperatures

23
Q

Arrhenius equation

A

K=Ae^-Ea/RT , where Ea= Enzyme activation energy

24
Q

What is am Arrhenius plot

A
  • Plot of LnK against 1/T
  • Gradient =-Ea/R
  • Y intercept =LnA
25
Q

What tend to be drugs

A

Enzyme inhibitors

e.g. Penicillin inhibits enzymes which enabe the bacteria to make a stable cross-linked cell wall.

26
Q

What is irreversible inhibition

A
  • Some inhibitors react covalently with essentil active site groups leading to permanent inactivation
    e. g. nerve gas
27
Q

What is reversible inhibition

A
  • Compounds bind non-covalently to enzymes, obstructing there activity
  • Can be removed by dilutions or dialysis
28
Q

How are Vmax and Km effected by competitive inhibitors

A
  • No affect on Vmax, but increases Km

- When there is a high S, S will displace the inhibitor, therefore E will always be saturated by S

29
Q

How are Vmax and Km effected by non-competitive inhibition

A
  • Vmax decreases but no affect on Km

- ESI complex is not able to generate product, therefore binding of I lowers catalytic activity

30
Q

Regulation by metabolites

A
  • End product inhibition

- Regulation by ATP/ADP/AMP concentrations of enzymes, control molecules bind to the regulatory site

31
Q

Regulation by regulatory proteins

A
  • 1:1 inhibitors
  • Interpreting signal, protein binds to a signal activating it, activated proteins bind to enzymes modifying their activities
32
Q

Regulation by reversible covalent modification

A

-Regulation by phosphorylation, attachment of phosphate group to OH groups

33
Q

Regulation by proteolysis

A
  • Some enzymes are made in an inactive form

- Cleavage of specific peptide bonds lead to their activation

34
Q

How do enzymes enhance specificity

A

change between alternate conformations

35
Q

Allosteric regulatiom

A
  • Co-operativity between identical active sites allows switching from inactive to active conformations
  • Binding of regulators to secondary sites allow them to affect this switching