MDCAT · CHAPTER 6
Enzymes
Understand what an active site really does, why rates change, and how competitive and non-competitive inhibitors differ.
Your study notes
01 / LESSON
Build the explanation.
- Explain how enzymes lower activation energy without changing equilibrium.
- Interpret effects of temperature, pH and substrate concentration.
- Compare competitive and non-competitive inhibition.
02 / NOTES
The essentials, in one place.
- Enzymes lower activation energy through an alternative pathway.
- Active sites depend on three-dimensional chemistry and induced fit.
- Saturation limits rate at high substrate concentration.
- Competitive inhibition differs from non-competitive inhibition in site and kinetic effect.
03 / ACTIVITY
Test the idea by changing something.
Predict the result first, run the activity, then explain what changed and why.
04 / DIAGRAM
Make the connections visible.
Substrate collides with the active site.
Specific interactions form an enzyme–substrate complex.
The transition state is stabilised.
Products leave; the enzyme is reusable.
Cover the labels, redraw the sequence or comparison, and explain each connection aloud.
See diagrams in the full explanation ↗05 / QUIZ
Retrieve before you reread.
Build a timed test from this chapter’s 100 practice questions. Questions and options are shuffled; missed answers feed your revision notebook.
Original practice items, including related concept variants; not official examination questions.06 / REVISION SHEET
Take the chapter away with you.
A print-friendly sheet brings together the learning targets, key points, concept diagram, written recall prompts and applied MCQs. Add the answer key when you are ready to check.
Print / save the chapter sheet ↗