Enzymes and Metabolism

Note Packet

Lesson Topic Essential Idea and Objective(s) IB Curriculum Connections Activities
1 Metabolism

Metabolism is the sum of the chemical reactions that occur within living organisms.

  • Define metabolism

Metabolic reactions can be intracellular or extracellular. 

  • State an example of an intracellular metabolic reaction (protein synthesis).

  • State an example of an extracellular metabolic reaction (chemical digestion in the alimentary canal). 

Metabolic processes may have a series of steps in the form of a metabolic pathway, which can be linear or cyclical.  

  • Contrast linear metabolic chain reaction pathways with cyclical reaction pathways.

  • State and example of a linear metabolic pathway (glycolysis; digestion of starch to maltose to glucose)

  • State and example of a cyclic metabolic pathway (Kreb’s cycle, Calvin cycle)

Metabolic processes can be anabolic or catabolic.  

  • Define anabolic and catabolic. 

  • State an example of an anabolic reaction and a catabolic reaction.

Metabolism is the web of all the enzyme-catalyzed reactions in a cell or organism (2.1.U4).

Metabolic pathways consist of chains and cycles of enzyme-catalyzed reactions (8.1.U1).

Initial Knowledge Audit (ICI)

Where are we now? slide

Metabolism notes

HHMI Amylase evolution DBQ

2 Enzyme Structure

Enzymes are globular proteins that act as catalysts by having an active site to which specific substrates temporarily bind by induced fit. 

  • Outline properties of globular proteins. 

  • Explain the relationship between enzyme structure and enzyme specificity, including the role of the active site.


Coenzymes and cofactors are molecules that help an enzyme to function appropriately. 

  • Define coenzyme and cofactor. 

  • State an example of a coenzyme and a cofactor.

Enzymes have an active site to which specific substrates bind (2.5.U1).

Enzyme structure notes

Review of enzyme structure

3 Enzyme Function

Each step in a metabolic pathway is catalyzed by a specific enzyme.

  • State the role of enzymes in metabolism.

  • Define catalysis.

Enzyme catalysis involves molecular motion and the collision of substrates with the active site. 

  • Outline the three stages of enzyme activity.

  • Explain the role of random collisions in the binding of the substrate with the enzyme active site.

  • Describe the induced fit model of enzyme action.

  • State that enzymes speed up chemical reactions without being altered, so can be reused.

Enzymes lower the activation energy by creating a new reaction pathway. 

  • Define activation energy.

  • State that activation energy is used to break or weaken bonds in the substrate. 

  • Explain the role of enzymes in lowering the activation energy of a reaction.

  • Interpret graphs showing the effect of lowering the activation energy by enzymes.

Enzyme catalysis involves molecular motion and the collision of substrates with the active site (2.5.U2).


Enzymes lower the activation energy of the chemical reactions that they catalyze (8.1.U2).

Enzyme function notes

Enzymes exposed (A&B)

Enzyme function role plays:

Named enzymes in IB Biology

A&B:  How 'super-enzymes' that eat plastics could curb our waste problem 

A&B:  Engineering enzymes to help solve the planet's plastic problem

A&B:  Wax worm saliva rapidly breaks down plastic bags, scientists discover
4 Enzyme Rate Factors

Temperature, pH and substrate concentration affect the rate of activity of enzymes. 

  • Explain the effects of temperature, pH and substrate concentration with reference to collision theory, temporary and permanent denaturation. 

  • State the effect of denaturation on enzyme structure and function.

  • Draw and interpret graphs showing the effects of temperature, pH and substrate concentration of the activity of enzymes.

Temperature, pH,and substrate concentration affect the rate of activity of enzymes  (2.5.U3).


Denaturation of proteins by heat or by deviation of pH from the optimum (2.4.A2).


Enzymes are denatured (2.5.U4).


Factors that affect enzymes notes

Graphing pH

Graphing temperature

A&B:  Heat Beaters reading

Enzyme assay simulation

5 Enzyme Inhibition

Enzyme action can be inhibited or promoted by the presence of other molecules that temporarily or permanently bind to them.

  • Define enzyme inhibitor.

Inhibitors can be either competitive or noncompetitive.  

  • Contrast competitive and noncompetitive enzyme inhibition.

  • State an example of a competitive inhibitor

  • State an example of a noncompetitive inhibitor 


The effect of a competitive inhibitor can be reduced by increasing substrate concentration, but this has no effect on noncompetitive inhibition. 

  • Explain why the rate of reaction with increasing substrate concentration is lower with a non-competitive inhibitor compared to a competitive inhibitor.


Metabolic pathways can be controlled by end-product inhibition.

  • Describe allosteric regulation of enzyme activity.

  • Outline the mechanism and benefit of end-product inhibition.

  • Illustrate end-product inhibition of the threonine to isoleucine metabolic pathway.


Advances in computing technology have led to rapid identification of potential enzyme inhibitors with pharmaceutical applications. 

  • Outline the use and benefits of the bioinformatics technique of chemogenomics in development of new pharmaceutical drugs.

  • Explain the use of databases in identification of potential new anti-malarial drugs.

Enzyme inhibitors can be competitive or noncompetitive  (8.1.U3).


Metabolic pathways can be controlled by end-product inhibition (8.1.U4).


End-product inhibition of the pathway that converts threonine is isoleucine (8.1.A1).


Distinguish different types of inhibition from graphs at specified substrate concentration (8.1.S2).


Developments in scientific research follow improvements in computing- developments in bioinformatics, such as the interrogation of databases have facilitated research into metabolic pathways (8.1.NOS).


Use of databases to identify potential new anti-malarial drugs (8.1.A2).


Enzyme inhibition notes

Inhibition handwritten notes

Enzyme inhibitors animation

Inhibition graphs

Simulations

Serengeti Rules (Sean Carroll book)

  • Only make enzymes when needed:  55-58

  • Regulation, metabolic chains = 60-63

  • Feedback inhibition = 67-68

  • Allosteric inhibition = 69-71

Aspirin as an irreversible enzyme inhibitor from TPWKY (45:20 - 49:15 reduces risk of blood clot formation in heart attack patients)

Quantitative Biology with Catalase Floating Disk Technique – Wandering through Prairie Wonders
6 Enzyme Experiments

Design an experimental investigation of a factor affecting enzyme activity. 

  • Identify the manipulated, responding and controlled variables in descriptions of experiments testing the activity of enzymes.

  • Explain the need to control variables in experimental design.

  • Describe three techniques for measuring the activity of an example enzyme.


Accurate, quantitative measurements in enzyme experiments require replicates to ensure reliability. 

  • Define quantitative and qualitative.

  • Determine measurement uncertainty of a measurement tool.

  • Explain the need for repeated measurements (multiple trials) in experimental design.


Calculate the rate of reaction for enzyme-controlled reactions. 

  • State two methods for determining the rate of enzyme controlled reactions.

  • State the unit for enzyme reaction rate.

  • Given data, calculate and graph the rate of an enzyme catalyzed reaction.

Design of experiments to test the effect of temperature, pH, and substrate concentration on the activity of enzymes (2.5.S1).


Experimental investigation of a factor affecting enzyme activity (Practical 3) (2.5.S2).


Experimental design-accurate, quantitative measurements in enzyme experiments require replicates to ensure reliability (2.5.NOS).


Calculating and plotting rates of reaction from raw experimental results (8.1.S1).


Measuring enzyme reaction rates

Intro to enzyme experimental techniques

Enzyme inquiry lab introduction

Enzyme lab posters

Enzyme Labs:

7 Industrial Applications

Immobilized enzymes are widely used in industry, such as in the production of lactose-free milk.

  • List industries that use commercially useful enzymes.

  • Explain how and why industrial enzymes are often immobilized. 

  • State the source of the lactase enzyme used in food processing.

  • State the reaction catalyzed by lactase.

  • Outline four reasons for using lactase in food processing.

Immobilized enzymes are widely used in industry (2.5.U5).


Methods of production of lactose-free milk and its advantages (2.5.A1).

Enzymes in Industry notes

Enzyme in industrial reading

Making milk for cats

Lactase lab (K. Foglia)

Cellulase lab

A&B:  Adam Garske: How designing brand-new enzymes could change the world
8 Unit Wrap Up and Review Not applicable Not applicable

Enzyme review slides

Kahoot review (ICTD)

Quizizz Review (OCI)

1 page-summary (OCI)

Final Knowledge Audit (ICI)

9 Assessment Not applicable Not applicable