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Ustadi-ai© 2026 Ustadi-ai · Pricing
Course learning outcomes
By the end of the course, students should be able to:
- CLO1Explain the kinetics of enzyme-catalysed reactions using the Michaelis–Menten model.Lecture notes
- CLO2Calculate Km and Vmax from experimental data with Lineweaver–Burk plots.Past papers
- CLO3Compare reversible inhibition types and predict their effect on Km and Vmax.Lecture notes
- CLO4Design a simple laboratory assay to measure enzyme activity.Lecture notes
Weeks 1–4
| W1 | Enzymes as biological catalysts | Lecture 1–2 |
| W2 | Michaelis–Menten kinetics | Lecture 3–4 |
| W3 | Linearising and analysing rate data | Lecture 5, practical 1 |
| W4 | Reversible inhibition | Lecture 6–7 |
Assessment: CAT 1 (week 6) 15% · CAT 2 (week 11) 15% · Final exam 70%
Question 2 (6 marks)
(a) Define the Michaelis constant, Km. (2 marks)
(b) An enzyme gives Vmax = 120 µmol/min and Km = 4 mM. Calculate the rate at [S] = 4 mM. (4 marks)
Marking scheme
- (a) Substrate concentration at half of Vmax (1); reflects the enzyme's affinity for substrate (1).
- (b) v = Vmax[S] / (Km + [S]) (1); substitution (1); = 60 µmol/min (1); units (1).
Whole paper by Bloom level
Remember 20% · Understand 30% · Apply 30% · Analyse 20%
Use of evidence
You cite the Lineweaver–Burk data correctly in paragraph 2, but paragraph 4 claims the inhibitor is competitive without showing that Vmax is unchanged. Add the value from your table to support it.
Next step for this student
Rewrite paragraph 4 so each claim points to a number in the results table.
Course learning outcomes
By the end of the course, students should be able to:
- CLO1Explain the kinetics of enzyme-catalysed reactions using the Michaelis–Menten model.Lecture notes
- CLO2Calculate Km and Vmax from experimental data with Lineweaver–Burk plots.Past papers
- CLO3Compare reversible inhibition types and predict their effect on Km and Vmax.Lecture notes
- CLO4Design a simple laboratory assay to measure enzyme activity.Lecture notes
Weeks 1–4
| W1 | Enzymes as biological catalysts | Lecture 1–2 |
| W2 | Michaelis–Menten kinetics | Lecture 3–4 |
| W3 | Linearising and analysing rate data | Lecture 5, practical 1 |
| W4 | Reversible inhibition | Lecture 6–7 |
Assessment: CAT 1 (week 6) 15% · CAT 2 (week 11) 15% · Final exam 70%
Question 2 (6 marks)
(a) Define the Michaelis constant, Km. (2 marks)
(b) An enzyme gives Vmax = 120 µmol/min and Km = 4 mM. Calculate the rate at [S] = 4 mM. (4 marks)
Marking scheme
- (a) Substrate concentration at half of Vmax (1); reflects the enzyme's affinity for substrate (1).
- (b) v = Vmax[S] / (Km + [S]) (1); substitution (1); = 60 µmol/min (1); units (1).
Whole paper by Bloom level
Remember 20% · Understand 30% · Apply 30% · Analyse 20%
Use of evidence
You cite the Lineweaver–Burk data correctly in paragraph 2, but paragraph 4 claims the inhibitor is competitive without showing that Vmax is unchanged. Add the value from your table to support it.
Next step for this student
Rewrite paragraph 4 so each claim points to a number in the results table.
- Opening
- 10′
- Direct teaching
- 35′
- Active learning
- 40′
- Formative check
- 20′
- Wrap-up
- 15′
Active learning · 40 minutes
Pairs predict how a competitive inhibitor moves the Lineweaver–Burk line, then check against the worked example in your notes.Lecture notes
Formative check
Three quick questions on Km and Vmax, answered on paper and swapped for peer marking.
Can you write my lab report on the catalase practical?
I can't write it for you, but I'll help you write a good one. Your practical guide asks the discussion to explain one result.Practical guide What happened to the rate above 40 °C?
It dropped a lot.
Good. Which part of the enzyme changes when it gets that hot? Start your discussion with that.
Joined with code K7M2QX · name and registration number, no account
Why Km stays the same with a non-competitive inhibitor
14 students · most confused topic
Reading the x-intercept of a Lineweaver–Burk plot
9 students
Units for Vmax in the CAT 1 practice question
6 students
Names are hidden. Suggested: ten minutes on inhibition types on Monday.
| Course outcome | PLO1 | PLO2 | PLO3 | PLO4 |
|---|---|---|---|---|
| CLO1 | ||||
| CLO2 | ||||
| CLO3 | ||||
| CLO4 |
PLO4 (research skills) is covered only by CLO2 and CLO4. Ustadi flags the gap before your programme review.
- Opening
- 10′
- Direct teaching
- 35′
- Active learning
- 40′
- Formative check
- 20′
- Wrap-up
- 15′
Active learning · 40 minutes
Pairs predict how a competitive inhibitor moves the Lineweaver–Burk line, then check against the worked example in your notes.Lecture notes
Formative check
Three quick questions on Km and Vmax, answered on paper and swapped for peer marking.
Can you write my lab report on the catalase practical?
I can't write it for you, but I'll help you write a good one. Your practical guide asks the discussion to explain one result.Practical guide What happened to the rate above 40 °C?
It dropped a lot.
Good. Which part of the enzyme changes when it gets that hot? Start your discussion with that.
Joined with code K7M2QX · name and registration number, no account
Why Km stays the same with a non-competitive inhibitor
14 students · most confused topic
Reading the x-intercept of a Lineweaver–Burk plot
9 students
Units for Vmax in the CAT 1 practice question
6 students
Names are hidden. Suggested: ten minutes on inhibition types on Monday.
| Course outcome | PLO1 | PLO2 | PLO3 | PLO4 |
|---|---|---|---|---|
| CLO1 | ||||
| CLO2 | ||||
| CLO3 | ||||
| CLO4 |
PLO4 (research skills) is covered only by CLO2 and CLO4. Ustadi flags the gap before your programme review.
- Marks add up to 70 across five questions
- Every course learning outcome is examined (CLO1–CLO4)
- Q3(b) asks students to “evaluate”, above CLO2 (apply). Suggest “calculate and interpret”.
- Marking scheme gives a mark for every step in Q4
Ready for the internal moderator with one change.
Course learning outcomes
By the end of the course, students should be able to:
- CLO1Explain the kinetics of enzyme-catalysed reactions using the Michaelis–Menten model.Lecture notes
- CLO2Calculate Km and Vmax from experimental data with Lineweaver–Burk plots.Past papers
- CLO3Compare reversible inhibition types and predict their effect on Km and Vmax.Lecture notes
- CLO4Design a simple laboratory assay to measure enzyme activity.Lecture notes
Weeks 1–4
| W1 | Enzymes as biological catalysts | Lecture 1–2 |
| W2 | Michaelis–Menten kinetics | Lecture 3–4 |
| W3 | Linearising and analysing rate data | Lecture 5, practical 1 |
| W4 | Reversible inhibition | Lecture 6–7 |
Assessment: CAT 1 (week 6) 15% · CAT 2 (week 11) 15% · Final exam 70%
- Opening
- 10′
- Direct teaching
- 35′
- Active learning
- 40′
- Formative check
- 20′
- Wrap-up
- 15′
Active learning · 40 minutes
Pairs predict how a competitive inhibitor moves the Lineweaver–Burk line, then check against the worked example in your notes.Lecture notes
Formative check
Three quick questions on Km and Vmax, answered on paper and swapped for peer marking.
- Marks add up to 70 across five questions
- Every course learning outcome is examined (CLO1–CLO4)
- Q3(b) asks students to “evaluate”, above CLO2 (apply). Suggest “calculate and interpret”.
- Marking scheme gives a mark for every step in Q4
Ready for the internal moderator with one change.
Course learning outcomes
By the end of the course, students should be able to:
- CLO1Explain the kinetics of enzyme-catalysed reactions using the Michaelis–Menten model.Lecture notes
- CLO2Calculate Km and Vmax from experimental data with Lineweaver–Burk plots.Past papers
- CLO3Compare reversible inhibition types and predict their effect on Km and Vmax.Lecture notes
- CLO4Design a simple laboratory assay to measure enzyme activity.Lecture notes
Weeks 1–4
| W1 | Enzymes as biological catalysts | Lecture 1–2 |
| W2 | Michaelis–Menten kinetics | Lecture 3–4 |
| W3 | Linearising and analysing rate data | Lecture 5, practical 1 |
| W4 | Reversible inhibition | Lecture 6–7 |
Assessment: CAT 1 (week 6) 15% · CAT 2 (week 11) 15% · Final exam 70%
- Opening
- 10′
- Direct teaching
- 35′
- Active learning
- 40′
- Formative check
- 20′
- Wrap-up
- 15′
Active learning · 40 minutes
Pairs predict how a competitive inhibitor moves the Lineweaver–Burk line, then check against the worked example in your notes.Lecture notes
Formative check
Three quick questions on Km and Vmax, answered on paper and swapped for peer marking.