Enzymes and Enzyme Kinetics

What this unit covers

The resources here follow enzymes from first principles to regulation. Mind maps such as Enzyme Classification set out the six classes: oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. The Enzyme Kinetics maps explain the Michaelis constant (Km) as the substrate concentration at half of Vmax, and why a high Km means low affinity for the substrate.

Where to start

Begin with a broad map, then move to detail.

1. Open the Enzyme Kinetics mind map to see substrate, product and enzyme-substrate complex laid out together.
2. Read the note What does the Km value really mean? to firm up the idea.
3. Try the quiz Enzyme Kinetics 1, then Enzyme Kinetics 2.
4. Move on to the quiz Enzyme Kinetics and inhibition and the map Competitive and Noncompetitive Inhibitors.

Regulation and classification

A tidy run of notes, flashcards and quizzes covers enzyme regulation. The note on irreversible covalent modification describes proteolytic cleavage, mostly in extracellular processes. The note on reversible covalent modification covers the making and breaking of a bond between a non-protein group and an enzyme. The quiz Enzyme Regulation - Allosteric Enzymes asks about cooperative behaviour and how it appears on a graph.

For naming, the flashcard deck Enzyme Commission Number pairs EC numbers with enzymes such as alkaline phosphatase and aspartate aminotransferase.

Using quizzes and maps together

Read a map first, then take a quiz on the same topic and note what you missed. Go back to the map for those branches. For exam-style practice, the MCAT enzymes flashcard deck is there, and the community has also shared past-paper style quizzes such as Enzymes Past Papers.

Where it fits

This unit sits in the strand Enzymes, Coenzymes and Bioenergetics, within Biochemistry. Teachers can pick a map or quiz to set as a ready-made task. Choose one resource today and see how far it takes you.