BCMB 204 Course Outline
BCMB 204 Course Outline
BCMB 204 Course Outline
COURSE SYLLABUS
Course Code and Title: BCMB 204: ENZYMOLOGY
Credits: Two (2) credits
INTRODUCTION:
This is an introductory course in enzymology. The course provides an opportunity for students to learn
the basic concepts necessary to understand how simple catalysts and complex enzymes accelerate and
regulate biological reactions. Topics covered include enzyme catalysis, mechanism, specificity,
kinetics, regulation and the purification and application of enzymes in industry, medicine and
agriculture.
COURSE DESCRIPTION:
Enzyme Kinetics: Equilibrium and steady state reactions; Michaelis-Menten model; Graphical
representation of data (e.g., Lineweaver-Burk and Hanes plots); Significance of Vmax and Km;
Effect of pH; temperature, and enzyme concentration on reaction rates; Enzyme inhibition:
Reversible (competitive, uncompetitive, noncompetitive) and irreversible enzyme inhibitors.
1
Regulation of Enzyme Activity: Substrate or product regulation (feedback inhibition, feed
forward activation); Allosteric modulation; Cooperativity; Covalent modification; Isoenzymes;
Proteolytic activation; Regulation of enzyme synthesis (lac and trp operons),
• Understand the importance of enzymes and how they are regulated in cellular reactions.
• Learn importance of enzymes to man.
LEARNING OUTCOMES:
• Students should be able to identify the class of an enzyme catalyzing a biological reaction.
• Students should be able to predict how temperature, pH, inhibitors, and other factors would
affect enzyme activity.
• Students should be able to understand the science and steps in purifying and storing an enzyme.
• Students should be able to use kinetics as the primary tool to deduce how catalysts work.
COURSE DELIVERY:
PLAGIARISM:
All students are expected to familiarize themselves with the University plagiarism policy. The
policy is available online at http://www.ug.edu.gh/aqua/policies-guidelines
COURSE SCHEDULE:
Dr. D. Oduro-Mensah
Week 1
Catalysis
• Thermodynamic considerations
• Methods for accelerating reactions
• Features of enzyme active site
2
Week 2
Catalysis
Weeks 4, 5 and 6
Kinetics of Enzyme reactions
Weeks 7 and 8
Enzyme inhibition
Weeks 9 and 10
Regulation of enzyme activity
• Fine control
• Substrate or product regulation
• Allosteric modulation
3
• Cooperativity
• Covalent modification
• Isozymes
• Proteolytic activation
• Coarse control
• Inducible operon (lac operon)
• Repressible operon (trp operon)
Weeks 11 and 12
Enzyme purification
• Enzyme extraction
• Purification strategies
• Quantitative evaluation of purification steps
• Course material will be delivered through slide projections, and video presentations.
EXAMINATIONS