J92P2Q6a - Summarise the characteristic properties of enzymes (13) Characteristic Properties Details Globular proteins consisting of amino acid

sequences that twist into a polypeptide helix and fold into a compact 3D shape.

Structure

Efficiency of Enzyme

Very efficient catalysts with high turnover number. Turnover number gives indication of speed at which the substrate molecules are being converted to products by a molecule of enzyme in one second when it is fully saturated with substrate E.g. Carbohydrate anhydrase turnover number is 60,000 per second Effective in minute quantities. Speed up reaction by lowering activation energy. Remains unaltered at the end of reaction Highly specific Specific to one type of substrate (Lock and Key hypothesis) or Specific to group of similar substrates (Induced-fit hypothesis) Conformation of enzyme active site responsible for specificity of enzyme.

Amount Required

Specificity (link to active site and hypotheses)

How enzyme affects reversible reactions

Enzymes can catalyse the reverse reaction if the conditions are changed. These conditions which determine which reaction should proceed are ph and concentrations of reactants. Enzymes do not alter point of equilibrium of reaction.

Factors Affecting Rate of Reaction Temperature pH [Substrate] Near of below 0C pH is the With all other Enzyme inactivated measure of factors kept amount of H constant, ions in a reaction rate is solution proportional to [substrate]
2010 Yishun JC H1 & H2 Biology Enzymes tutorial (Essay answer key)

[Enzyme] With all other factors kept constant, reaction rate is proportional to [enzyme].
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Increasing temp temp, KE, Effective collisions, ES Complex, Product, Reaction Rate Optimum temp - High KE - Max Effective Collisions - Max ES Complex - Max Product - Max Reaction Rate Above Optimum Temp Intermolecular bond stabilising secondary and tertiary bonds disrupted Unfolding of enzyme molecule, active site shape lost Irreversible loss of enzyme structure and function Graph

Optimum pH - Intermolecular bonds intact - Max reaction rate Higher / Lower pH concentration of H+ ions is altered charges on R groups of amino acid residues of enzyme altered Ionic and H bonds maintaining 3D conformation of enzyme disrupted substrate cannot bind to altered active site of enzyme Enzymes work over narrow pH range

At low [substrate], rate of reaction is limited by [substrate]. [substrate] effective collisions ES Complex, Product, Reaction Rate - until saturation point this is when [enzyme] is limiting

At low [enzyme], Rate of reaction is limited by [enzyme] [enzyme] effective collisions ES Complex, Product, Reaction Rate - until saturation point this is when [substrate] is limiting

Graph

Graph

Graph

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Summarise End-product Inhibition (3)

A metabolic pathway usually involves a series of reactions in which each is catalysed by an enzyme. When the end product of a metabolic pathway begins to accumulate, it may act as an inhibitor, usually on the enzyme catalyzing the first reaction in the pathway. As a result, the final product is able to switch off its own production as it builds up. This process is self regulatory: as the product is used up, the inhibition is lifted and the production is switched back on again. End product inhibition is a form of negative feedback.

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J96P3Q7 (a) Describe the protein structure of an enzyme. [max 6] An enzyme is a complex three-dimensional globular protein. Its primary structure has a unique sequence of amino acids. The secondary structure of an enzyme is either an -helix or -pleated sheet stabilized by hydrogen bonds. The binding and folding of the enzymes secondary structure gives it its globular shape. Disulphide bonds, hydrogen bonds, ionic bonds and hydrophobic interactions maintain the tertiary structure. Only a small region of the enzyme (~3 to 12 amino acid residues) comes into direct contact with the substrate. This region is called the active site. The amino acid residues at the active site are divided into 2 groups: the contact residues and the catalytic residues. The contact residues gave the enzyme its specificity and form a shape that is complementary to the shape of the substrate. The catalytic residues act on the bonds in the substrate which are broken by enzyme action. An enzymes activity can be altered by molecules acting at a site other than the active site called an allosteric site. The binding of a regulatory molecule to the allosteric site changes the overall shape of the enzyme. This can enable or prevent the binding of a substrate to the active site.

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(b) Distinguish between competitive and non-competitive inhibition of enzymes. [max 7]

2010 Yishun JC H1 & H2 Biology Enzymes tutorial (Essay answer key)

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Features Structure of inhibitor

Competitive inhibitor Have close structural resemblance to the substrate.

Non-competitive inhibitor

Have

no close structural resemblance to the substrate.

Site of binding of inhibitor

Binds to active site of the enzyme. bonding is temporary.

The

Binds to a region other than active

site of the enzyme. The bonding is permanent. Normal formation of an enzymesubstrate complex.

Competitive inhibitor bounded to active site. Formation of enzyme-substrate complex inhibited.

Effect of increasing substrate concentration on inhibition on the rate of reaction

Inhibition can be reversed because substrate molecules can displace the inhibitor from the active site of enzyme.

No effect as the bonding between the enzyme and inhibitor is irreversible.

Maximum rate of reaction

At very high substrate concentration, the maximum rate of reaction in the presence of inhibitor can be very close to that of reaction in the absence of inhibitor.

Even at very high substrate concentration, the maximum rate of reaction in the presence of inhibitor is less than that of reaction in the absence of inhibitor.

Graph showing effect of the inhibitor on relationship between rate of reaction and substrate concentration 2010 Yishun JC H1 & H2 Biology Enzymes tutorial (Essay answer key) Page 6

Confusion: Active site of enzyme is found on the substrate molecule.

(c) Explain the effects of enzyme and substrate concentration on the rate of enzyme catalysed reactions. [5] Effects of substrate concentration on the rate of enzyme-catalysed reactions: For a fixed enzyme concentration, the rate of reaction increases with increasing substrate concentration. An increase in the number of substrate molecules will result in an increase in the frequency of successful collisions between enzyme and substrate molecules. More enzyme-substrate complexes will be formed and the rate of reaction will increase. Here, the rate of reaction is limited by substrate concentration. Increasing the substrate concentration increases the rate of reaction linearly. When all the active sites of the enzyme molecules are saturated with substrate molecules, any further increase in substrate concentration will not produce a significant change in enzyme action. The rate of reaction is now limited by enzyme concentration.

Effects of enzyme concentration on the rate of enzyme-catalysed reactions: An increase in enzyme concentration will increase the rate of reaction, provided there is no other limiting factor. At very high enzyme concentrations, if the concentration of substrate molecules is limiting, an increase in enzyme concentration would not result in any further increase in the rate of reaction.

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