Enzymes

Enzymes

Structure
1. Protein
2. Tertiary - Quaternary
  1. Folded
3. 3D, Globular
4. Specific
Factors
1. Temperature
  1. Optimum temperature
    1. Temperature enzyme works most efficiently at
  2. Too cold
    1. Slower rate of reaction
      1. Less energy
  3. Too hot
    1. Denaturing
      1. Temperature causes H bonds to seperate
        Chain becomes unfolded
        Active site changes shape
2. PH
  1. Optimum PH
  2. Too high PH (alkaline)
    1. Slower rate of reaction
  3. Too low PH (acidic)
    1. H- ions and ionic bonds affected by H+ ions
      1. Denaturing
  4. Measure of H ion concentration
3. Inhibition
  1. Competitive
    1. Inhibitor has similar structure to substrate
      1. Competes for active site of the enzyme
  2. Non competitive
    1. Inhibitor binds to site other than active site
      1. Causes conformational change
Models
1. Induced fit
  1. Enzyme + substrate do not perfectly fit
    1. But structure is complementary
      1. Substrate binds to active site
        Causes conformational change
        Enzyme "moulds" around substrate
        Enzyme catalyses reaction
2. Lock and Key
  1. Enzyme + substrate fit perfectly
    1. Structure is perfectly complementary
      1. Substrate binds to active site
        Enzyme catalyses reaction
Properties
1. Types
  1. Builders
    1. Joins molecules together
  2. Breakers
    1. Breaks molecules down
2. Biological catalysts
  1. Speeds up reactions
3. Not used up during reaction
Examples
1. (Substrate)
  1. Starch
    1. Maltose
      1. Lactose
2. (Product(s))
  1. Maltose
    1. a glucose
      1. Glucose
      2. Galactose
3. (Enzyme)
  1. Amylase
    1. Maltase
      1. Lactase

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