Session 3 ILOs - Enzymes Flashcards

1
Q

State the key features of enzymes

A

Enzymes are catalysts which increase the rate of reaction
They do NOT alter the equilibrium of a chemical reaction - they simply increase the rate at which the equilibrium is reached
Work by lowering the activation energy for a reaction

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2
Q

Explain the role of the active site of an enzyme

A

The active site allows a substrate to bind to the specific region of an enzyme & forms the enzyme-substrate complex.
The active site is formed by amino acids from different parts of the primary sequence and reaction between the enzyme and the substrate is stabilised by surrounding amino acids within the active site
Substrates are bound to enzymes by weak bonds therefore allows the products to be released

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3
Q

Describe how reaction rates vary as a function of enzyme concentration (assuming substrate concentration stays the same)

A

Rate of an enzyme-catalysed reaction is proportional to the enzyme concentration i.e. if you double conc. of enzyme, the rate of reaction doubles

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4
Q

Describe how reaction rates vary as a function of substrate concentration (assuming enzyme concentration stays the same)

A

Rate of an enzyme-catalysed reaction increases as the substrate concentration increases, however this does plateau as the enzymes become saturated

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5
Q

Define the 2 terms of activity & international unit of enzyme activity

A

Vmax and Vo are rates of activity

1 unit = the amount of enzyme that produces 1umol of product per min under standard condition

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6
Q

Define Vmax & Km

A
Vmax = theoretical maximum rate of reaction when all of the enzyme molecules are saturated with substrate and they are proceeding as quickly as they can
Km = substrate concentration that gives half the maximal rate of reaction (Vmax)
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7
Q

Describe the effects of the 2 types enzyme inhibitors on their kinetics and be able to between the two from simple graphs

A

Competitive inhibitor (binds at active site) & non-competitive inhibitor (binds at site away from the active site)

  1. Competitive inhibitors
    Km increases, Vmax unaffected
  2. Non-competitive inhibitors
    Km unaffected, Vmax decreases
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