ENZYMES

Biological Catalysts

Globular Proteins

 State that enzymes are globular proteins with a specific tertiary structure. State that enzymes catalyse metabolic reactions in living organisms.

Primary structure to tertiary structure in enzymes

Commercial application of enzymes

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 State that enzyme action may be extracellular or intracellular.

Mould produces extracellular enzymes to digest bread

Lysosome and phagocytosis

Names of Enzymes
Either type of reaction catalysed E.g. Carboxylase Dehydrogenase E.g. Amylase, Protease

Name of Substrate Add the suffix ase EXCEPTION ?

PEPSIN

 State that enzymes are globular proteins with a specific tertiary structure. State that enzymes catalyse metabolic reactions in living organisms.

 Describe the mechanism of enzyme action with reference to specificity, active site, lock-andkey and induced-fit hypotheses. Explain what is meant by enzymesubstrate complex and enzymeproduct complex. Describe how enzymes lower the activation energy of a reaction.

PROPERTIES OF ENZYMES SPECIFICITY

i.e. each enzyme will only catalyse ONE reaction
OR, put another way,

EACH reaction requires a DIFFERENT enzyme

HOW DO ENZYMES WORK ?

THE LOCK AND KEY MECHANISM

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The lock-and-key hypothesis

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The induced-fit hypothesis

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OR
IN THREE DIMENSIONS :

Enzyme specificity depends on:

1.Tertiary structure of enzyme determines 3D structure 3.Shape of active site determines specificity of enzyme

2.Tertiary structure forms active site

4.If tertiary structure is damaged, enzyme may not function

Enzyme specificity depends on:

1.Tertiary structure of enzyme determines 3D structure 3.Shape of active site determines specificity of enzyme

2.Tertiary structure forms active site

4.If tertiary structure is damaged, enzyme may not function

Complementary fit between active site and substrate

Correct shape fits; others will not

Substrate and enzyme change shape slightly on binding puts strains on bonds

Weakens bonds, lowers activation energy, making reaction more likely

HOW DO ENZYMES ACTUALLY SPEED UP REACTIONS ?

They are said to lower the ACTIVATION ENERGY

Activation energy (maltose to glucose)

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How the enzyme maltase lowers the activation energy needed to convert maltose to glucose

 Enzymes and metabolism an overview

A metabolic pathway

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Phenylketonuria sequence and effects

FACTORS WHICH AFFECT ENZYME ACTIVITY

ENZYME CONCENTRATION TEMPERATURE

SUBSTRATE CONCENTRATION

pH

TEMPERATURE

Describe and explain the effect of temperature changes on enzyme activity.

Random movement of dissolved maltose molecules in solution

Random collisions between maltose, maltase and water molecules

How denaturation changes enzyme structure

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The effect of temperature on the rate of an enzyme-controlled reaction

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 Describe and explain the effects of enzyme concentration and substrate concentration on enzyme activity.

ENZYME CONCENTRATION

Effect of enzyme concentration on the rate of an enzyme-controlled reaction

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SUBSTRATE CONCENTRATION

Effect of substrate concentration on the rate of an enzyme-controlled reaction

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pH

 Describe and explain the effects of pH changes on enzyme activity.

Proton donors

Tertiary structure bonds and interference with hydrogen ions

Active site charges and + H clustering

Optimum pH graph versus rate of reaction

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Pepsin and trypsin rate graph

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 Describe how the effects of pH, temperature, enzyme concentration and substrate concentration on enzyme activity can be investigated experimentally.

Measuring enzyme activity TWO APPROACHES

1. Measure rate of APPEARANCE of PRODUCT 2. Measure rate of DISAPPEARANCE of SUBSTRATE

Rate of APPEARANCE of PRODUCT

EXAMPLE

Activity of CATALASE

2H2O2 -------------> 2H2O +

O2

Measure volume of oxygen produced per unit time

Apparatus for measuring catalase activity

Rate of DISAPPEARANCE of SUBSTRATE

EXAMPLE

Activity of AMYLASE

Starch (Amylose) -------------->

Maltose

Measure loss of starch per unit time

Using starch plates to measure enzyme activity

Initial reaction rate comparisons

ENZYME INHIBITORS
May be

COMPETITIVE
OR

NON-COMPETITIVE
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COMPETITIVE INHIBITORS
Similar shape to normal substrate Compete with substrate for access to active site May fit into active site instead of substrate Substrate is therefore blocked from the active site So enzyme-substrate complex cannot form Effect depends on balance between amount of inhibitor and amount of substrate

NON-COMPETITIVE INHIBITORS
Are NOT similar shape to substrate so do NOT fit into active site
Attach to the enzyme elsewhere (ALLOSTERIC EFFECT) Causes enzyme shape to distort including the active site

So substrate can no longer fit

Increasing substrate concentration will NOT reverse the effect

Examples : Some antibiotics and sulphonamide drugs Malonic acid inhibits succinic acid dehydrogenase

Examples : Heavy metals arsenic, mercury, lead Cyanide inhibits cytochrome oxidase