Enzymes

ENZYMES are proteins that catalyses specific reactions. Basic mechanism involved

binding of the substrate(s) to the active site on the enzyme.

Active site:: specific region of the enzyme which combines with the substrate.

Enzymes and chemical catalyst

They differ in: 1) Higher reaction rates by enzyme 2) Enzymes catalysed reaction happened in milder conditions 3) Enzymes catalysed specific reactions and do not produce side products 4) Catalytic activities by enzymes varied by [substances]

Descriptions of shapes of enzymes

Water-soluble globular proteins Active site recognized certain substrate. Specificity determined by chemical nature of the amino acids R-groups located at the active site. Active site occupies < 5% of enzyme surface area and involves 3 to 12 amino acids.

The key and lock model

Proposing by Fischer Enzymes catalysed reactions by binding to substrates The substrate (key) fits into enzyme (lock) Once the product formed, they leave the active site and the enzyme is free to combine with new substrate.

Competitive Inhibition
Competitive inhibitors are substrate that have a similar shape to the substrate molecule. Can bind to the active site but cannot take part in the catalysed reaction. Reversible by increasing concentration of substrate.

Non-competitive Inhibition (1)

Inhibitor does not bind to the active site but other position on the enzyme. The binding of inhibitors caused one of these: 1) The active site to change shape so that substrate cannot bind 2) The enzyme-substrate complex to change shape so that reaction cannot take place.

Non-competitive Inhibition
Most non-competetive inhibitors bind weakly to the enzyme [Inhibitors] falls, enzyme-inhibitor complex falls apart and the functional shape of the enzyme restored. Reversible Eg heavy metal like Ag or Hg can replace H in one or more SH group, it change the shape of the enzyme.

Factors affecting enzyme activity

1. Temperature affect speed, activation energy of the catalysed rxn, thermal stability of the enzymes and substrate. 0 to 40 C, rate increase with T. Optimum at 40 C, decrease above 40 C. heat denatured at 65 C.

2. pH extreme pH will denature proteins by disrupting the precise 3-D arrangement of the protein chains. Small changes in pH affect the ionisation of amino acid side-chains in the active site. Each enzyme has its own distinct optimum pH. Eg figure 1.27 pg 23.

3. Chemical denaturation High salt concentration changes the ionic environment of an enzyme, disrupting the ionic interactions between different regions of the chain. Urea denatures protein by disrupting the Hbonds that maintain the secondary and tertiary structure of proteins.

 Certain chemical inhibitors totally inactivate enzymes, it means their effect is irreversible. Eg DFP binds to serine in active sites of chymotrypsin. Sarin (nerve gas) is very similar in structure to DFP.

ALCOHOL

In the secondary structure, hydrogen bonding occurs between amides. In the tertiary structure, hydrogen bonding between "side chains" occurs All these bonds are disrupted by the addition of the OH functional group.