Course code:
431B1		 Course name:
Enzymology

Academic year:

2019/2020.

Attendance requirements:

(001A1 + 029B1) / 401B1

ECTS:

7

Study level:

basic academic studies

Study program:

Biochemistry: 3. year, winter semester, compulsory course

Teacher:

Jelena Z. Radosavljević, Ph.D.
assistant professor, Faculty of Chemistry, Studentski trg 12-16, Beograd

Assistant:

Marija B. Peruško, Ph.D.
research associate, Innovation center, Studentski trg 12-16, Beograd

Hours of instruction:

Weekly: two hours of lectures + one hour of exercises + four hours of labwork (2+1+4)

Goals:

The main goal of this course is to help students acquire the basic knowledge of enzyme kinetics and the mechanism of enzyme action and catalysis. They will also learn about the application of enzymes in biotechnology, food industry and pharmaceutical industry. Students will also learn how to solve some problems in the area of enzyme kinetics.

Outcome:

Students have acquired the basic knowledge and skills in enzyme kinetics and the mechanism of enzyme action and catalysis. Students can solve problems in the area of enzyme kinetics.

Teaching methods:

Lectures. Exercises. Revision. Theory exercises.

Extracurricular activities:

—

Coursebooks:

Main coursebooks:

  • Alan Fersht: Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding (W. H. Freeman and Company, New York, 1999)
  • Đorđe Petrović: Enzimologija (Zavod za udžbenike i nastavna sredstva, Beograd, 1998)

Supplementary coursebooks:

  • Radivoje Prodanović, Tanja Ćirković Veličković: Enzimologija: Laboratorijski priručnik (Hemijski fakultet Univerziteta u Beogradu, 2005)
  • Ivanka Karadžić: Izračunavanja u enzimologiji
  • Haruo Suzuki: How Enzymes Work: From Structure to Function (CRC Press Book, 2015)

Additional material:

http://helix.chem.bg.ac.rs/~tcirkov/1421B-Enzimologija/

  Course activities and grading method

Lectures:

5 points (2 hours a week)

Syllabus:

  • Introduction to enzymology and enzyme catalysis.
  • Biological catalysts: structure, function, catalytic properties.
  • Methods used for the isolation and purification of enzymes.
  • The active site. Enzyme specificity.
  • Chemical kinetics. Enzyme kinetics of monosubstrate reactions.
  • Enzyme kinetics of multisubstrate reactions.
  • The inhibition of enzyme activity.
  • The effect of pH and temperature on enzyme activity.
  • The regulation of enzyme activity. Allostery.
  • The mechanism of enzyme action (family of serine proteases, lysozyme, other examples).
  • Applied enzymology (some examples of enzymes which are applied in molecular biology techniques, clinical enzymology, biotechnology and food industry).

Exercises:

5 points (1 hour a week)

Labwork:

10 points (4 hours a week)

Syllabus:

  • Basic determinations in enzymology: enzyme units and enzyme activity assays.
  • Basic determinations in enzymology: kinetic determinations of substrate specificity, Km and Vmax for monosubstrate enzymatic reactions.
  • Basic determinations in enzymology: kinetic determinations of the constant and the type of enzyme activity inhibition.
  • The effect of temperature and pH on enzyme activity and stability.
  • Determination of Km and Vmax for bisubstrate enzymatic reactions.

Colloquia:

30 points

Written exam:

20 points

Oral exam:

30 points