BCH 312 - Enzymology COURSE PARTICULARS Course Code: BCH 312 Course Title: Enzymology No. of Units: 3 Course Duration: Three hours of per week for 15 weeks. Status: Compulsory Course Email Address: mmekperigin@futa.edu.ng Course Webpage: http://www.fwt.futa.edu.ng/courseschedule.php?coursecode=fwt%20312 Prerequisite: NIL COURSE INSTRUCTORS Dr (Mrs) M. M. Ekperigin Room 101, School of Sciences Building, Dept. of Biochemistry, Federal University of Technology, Akure, Nigeria. Phone: +2348029503476 Email: mmekperigin@futa.edu.ng and Dr. D. M. Sanni Room 203, School of Sciences Building, Dept. Biochemistry, Federal University of Technology, Akure, Nigeria. Phone: +2348069256694 Email: dmsanni@futa.edu.ng COURSE DESCRIPTION This course is an introductory and the first course in enzymology designed specifically for students in biochemistry. The course will cover a wide range of subjects such as vitamins and coenzyme, classification of enzyme, mechanism and kinetics of enzyme catalyzed reaction. The final part will deal with the production, extraction, purification, characterisation and application of enzymes. 1
COURSE OBJECTIVES The objectives of this course are to: introduce students to various theoretical and practical aspects of enzymology; and stimulates their interest in learning the structure, function and kinetics of enzyme and their role as catalyst and regulator of cell metabolism. serve as foundation for more advanced enzymology courses. COURSE LEARNING OUTCOMES / COMPETENCIES Upon successful completion of this course, the student will learn: (Knowledge based) the major classes of enzyme and their functions in the cell; role of co-enzyme cofactor in enzyme catalyzed reaction; Differentiate between equilibrium and steady state kinetics and analyzed simple kinetic data and estimate important parameter (Km. Vmax, Kcat etc); to define and describe the properties of enzymes in and regulates biochemical pathways (inhibition, allosterism); GRADING SYSTEM FOR THE COURSE This course will be graded as follows: Assignments 20% Test(s) 20% Final Examination 60% TOTAL 100% GENERAL INSTRUCTIONS Attendance: It is expected that every student will be in class for lectures. Attendance records will be kept and used to determine each person s qualification to sit for the final examination. In case of illness or other unavoidable cause of absence, the student must communicate as soon as possible with any of the instructors, indicating the reason for the absence. Academic Integrity: Violations of academic integrity, including dishonesty in assignments, examinations, or other academic performances are prohibited. You are not allowed to make copies of another person s work and submit it as your own; that is plagiarism. All cases of 2
academic dishonesty will be reported to the University Management for appropriate sanctions in accordance with the guidelines for handling students misconduct as spelt out in the Students Handbook. Code of Conduct in Lecture Rooms: Students should turn off their cell phones during lectures. Students are prohibited from engaging in other activities (such as texting, watching videos, etc.) during lectures. Food and drinks are not permitted in the classroom. READING LIST 1 David Nelson and Micheal Cox, Leninger Principle of Biochemistry, Fifth edition W.H Freeman &Co., Newyork. 1 Stryer, L, Biochemistry, Fifth edition W. H Freeman & Co., Newyork. 4 Palmer,T and Bonner, P Enzymes: Biochemistry, Biotechnology and Clinical Chemistry Second edition. 4 Alan Fersht, Structure and Mechanism in Protein Science, Second edition W.H Freeman & Co. Newyork. Legend 1- Available in the University Library 2- Available in Departmental/School Libraries 3- Available on the Internet. 4- Available as Personal Collection 5- Available in local bookshops. 3
COURSE OUTLINE Week Topic Remarks 1 Introduction and General Overview Of the course History and discoveries of enzymes Chemistry and functions of enzyme in the cell Nature of enzyme and non-protein factor 2 & 3 Introduction to vitamins and co-enzymes Fat and water soluble vitamins Classification of co-enzymes Structure and functions of vitamins and Students will be informed of the important of regular class attendance and the grading system for the course Students should learn the structure and function of the vitamins. coenzymes 4 Classification and nomenclature of enzymes Students expected to know Enzyme Commission nomenclature and important representatives of each class of enzymes. 5 & 6 Kinetics of enzyme catalyzed reactions, Michealis- Menten equation, Estimation of kinetic parameters km, Vmax, Kcat etc Emphasis will be on single substrate/products model, students are expected to understand the significant of kinetic constant 7& 8 Inhibition of enzymes. Type of inhibitors Estimation of Ki Students are expected to understand the different inhibition types and their effect on enzyme reaction rate. 9 & 10 Mechanisms of enzyme-catalyzed reaction. Transition state theory Effects of Temperature ph ionic strength and inhibitors on enzyme catalysed reactions. TEST Students are expected to know the effect of these factors on enzyme activity. 4
11 Allosteric / Regulatory enzymes Sigmoidal kinetics Students are expected to understand the advantage of allosterism with respect to regulation of enzyme activities and metabolic pathways. 12 Active sites of enzymes Zymogen activation Digestive enzymes Students are expected to know the nature of active site and the amino acid residues important in catalysis. 13 &14 Production and isolation(production of enzyme from Animal, microbial and plant sources) and purification ( salt precipitation, centrifugation and chromatographic methods), characterisation of enzymes Recent advances in enzymology 15 Revision There are no laboratory experiments but students are expected to understand the different methods of isolation and purification and assays of enzyme 5