Enzymes & Your Body By Malinda Pires

First, some key terms

Enzyme: large protein that acts as a catalyst for biochemical reactions. Substrate: reactant in a biochemical reaction Active site: region on the surface of an enzyme to which substrates bind and which catalyses the chemical reaction between substrates.

Enzymes are Catalysts

Enzymes speed up chemical reactions. Each enzyme is specific to a certain substrate due to the shape of its active site Animation Menu Enzymes are catalysts to over 4000 biochemical reactions!

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Enzymes are Reusable

Enzymes are reusable molecules found in living things. They speed up biochemical reactions but are not changed by the reaction themselves, so they can be reused over and over again.

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Classifying Enzymes
There are 4 major categories of macromolecules: carbohydrates, lipids, proteins, & nucleic acids

1 http://en.wikipedia.org/wiki/File:Glucose-2D-skeletal.png 3 http://en.wikipedia.org/wiki/File:Mouse-cholera-antibody-1f4x.png

2 http://en.wikipedia.org/wiki/File:Phospholipids_aqueous_solution_structures.svg 4 http://en.wikipedia.org/wiki/File:Benzopyrene_DNA_adduct_1JDG.png

Most enzymes belong to the class of proteins. However, there are a few catalytic RNA molecules.
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Naming Enzymes
Take the name of the substrate the enzyme works on and add the suffix -ase Example: Lactose Lactase

http://en.wikipedia.org/wiki/File:Lactase.jpg

Life Sciences-HHMI Outreach. Copyright 2009 President and Fellows of Harvard College

Lactose Intolerance
When a persons body does not make enough lactase, lactose builds up in their digestive system and is digested by bacteria in the intestines. The bacteria produce gas as part of the digestion of lactose and that is why people with lactose intolerance may experience abdominal cramps, bloating and gas after consuming products with lactose (i.e.dairy)

Solutions
Lactose free milk lactase is added to cows milk and breaks down the lactose to glucose and galactose. Lactaid lactase in pill form. Taking a few lactase pills before consuming dairy allows people with lactose intolerance to digest small amounts of dairy products.

Enzyme Form and Function

Lock & key Model: The shape of an enzyme allows it to do a specific job much like a lock and key. Specificity - Animation Menu

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http://en.wikipedia.org/wiki/File:Wardedlock.jpg

Life Sciences-HHMI Outreach. Copyright 2009 President and Fellows of Harvard College

Limitations of the lock and key model

Some enzymes can catalyze more than one reaction The Induced fit model explains how the active site of an enzyme can sometimes fit more than one type of substrate

Induced Fit Model

As the substrate approaches the enzyme, it induces a conformational change in the active site i.e. the active site changes shape to fit the substrate. The bonds in the substrate become stressed, reducing the activation energy required for the reaction to occur. Animation

Denaturing Enzymes
When an enzyme is denatured it is damaged. Denaturing changes the shape of the active site. Without the correct shape enzymes wont function properly. HOW are enzymes denatured? Temperature and pH Animation Menu
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Effect of temperature, pH and substrate concentration

Predict the effect of changes in temperature, pH and substrate concentration on the rate of reaction catalyzed by an enzyme. Draw a graph of your prediction with the independent variable (temperature, pH etc) on the x-axis and rate of reaction on the yaxis.

Effect of temperature

Effect of pH

Effect of substrate concentration

Enzyme inhibition
Some chemical substances bind to enzymes and reduce the activity of the enzyme. These are called inhibitors. There are two types of inhibitors: competitive inhibitors and noncompetitive inhibitors

Competitive Inhibition
The inhibitor binds reversibly to the enzymes active site. While it remains bound, substrates cannot bind.

Non-competitive inhibition
The inhibitor binds reversibly to a site away from the active site. While it remains bound, the active site is distorted and the substrate cannot bind.

Enzymes are used all over your body!

http://en.wikipedia.org/wiki/File:Digestive_system_diagram_en.svg

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http://upload.wikimedia.org/wikipedia/commons/thumb/6/6f/Major_digestive_enzymes.png/750px-Major_digestive_enzymes.png

Life Sciences-HHMI Outreach. Copyright 2009 President and Fellows of Harvard College

Data Based Question: the Effectiveness of Enzymes

The degree to which enzymes increase the rate of reactions varies greatly. By calculating the ration between the rate of reactions with and without an enzyme catalyst, the affinity between an enzyme and its substrate can be estimated. Table 2 shows the rates of four reactions with and without an enzyme. The ratio between these rates has been calculated for one of the reactions.

Enzyme

Rate without catalyst/ s-1

1.3 x 10-1 1.7 x 10-7 1.7 x 10-13 2.8 x 10-16

Rate with enzyme/s-1

1.0 x 106 6.4 x 104 9.5 x 106 3.9 x 108

Ratio between rate with and without enzyme

7.7 x 106

Carbonic anhydrase Ketosteroid isomerase Nuclease OMP decarboxylase

1) State which enzyme catalyzes the reaction with the slowest rate in the absence of an enzyme. (1) 2) State which enzyme catalyzes its reaction with the most rapid rate. (1) 3) Calculate the ratios between the rate of reaction with and without an enzyme for ketosteroid isomerase, nuclease and OMP decarboxylase. (3) 4) Discuss which of the enzymes is the more effective catalyst (3) 5) Explain how the enzymes increase the rate of the reactions they catalyze (2)