Biochemistry & Enzymolozy

Paper Code: 
MBL 122
Credits: 
05
Contact Hours: 
75
Objective: 

To enable students to- • understand the chemistry of biomolecules • Understand the bioenergetic principles underlying biochemical reactions. • Understand the structure, mechanism of action and inhibition of enzymes.

10.00
Unit I: 
Chemical foundations of Biology

pH, pK, acids, bases, buffers, chemical bonds, Bioenergetics: Principles of thermodynamics: free energy, important energy, rich molecules, standard free energy change, concept of redox reactions. Principles of self assembly, Hierarchy of molecular organization of living systems

15.00
Unit II: 
Amino acids and proteins

Amino acids, Classification, Chemical Reactions and Physical Properties, Proteins-purification and criteria for homogeneity, structural organization of proteins- primary, secondary, tertiary and quaternary structure. Conformational analysis. Ramachandran plot.

15.00
Unit III: 
Carbohydrates

Classification and reactions, types, structural features. Metabolism of carbohydrates, main sources of carbohydrates, enzymatic conversion and mobilization as glucoses or fructoses, glycolysis, Krebs cycle, terminal oxidation/ oxidative phosphorylation, mechanism of ATP synthesis, rate controlling steps and regulation.

15.00
Unit IV: 
Lipids

Classification, Structure and functions. Metabolism of Lipid and fat bodies: Beta-oxidation and channeling of the products to ATP production: minor pathway of fatty acid oxidation, (alpha and omega oxidation), Biosynthesis of saturated and unsaturated fatty acids, Ketone bodies, membrane lipids-cholesterol, phospholipid and glycolipid; biosynthesis of fat soluble vitamins; biosynthesis of Eicosonoids (prostaglandin, leucotriens and thromboxane).

20.00
Unit V: 
Enzymes

Kinetics: Rate of reactions, specific activity, molecular activity, Km, Kcat, Michaelis –Menten & Line weaver Burk plot and Bisubstrate Reaction, enzyme inhibition, mechanism of enzyme catalysis (acid-base electrostatic, metal ion, free radicals, transition state binding and covalent, proximity and orientation effects, Contribution of strain). Factors affecting enzyme activity, enzyme inhibition. Allosteric enzymes in bisubstrate reactions. Enzyme Engineering.

ESSENTIAL READINGS: 

1. Biochemistry, D.Voet and J.G.Voet, John Wiley & Sons, (2nd Edition), 1995. 2. Principles of Biochemistry, Lehninger ,Nelson and Cox, (3rd Edition), 1999. 3. Principles and Techniques in Biochemistry and Molecular Biology, Edited by Keith Wilson and John Walker, Cambridge University Press, (6th Edition), 2007. 4. Biochemistry and Molecular Biology by W.H. Elliot and Daphne C. Elliot, Oxford University Press, (3rd Edition), 2005. 5. Biochemistry, J. David Rawn, Panima Publishing Corporation, 1st Indian Reprint, 2004.

REFERENCES: 

1. Physical Biochemistry, D Friefelder, W.H. Freeman & Company, 17th Reprint, 1999. 2. Understanding Chemistry, CNR Rao, University Press, Hyderabad 1999. 3. A Biologist's Guide to Principles and Techniques of Practical Biochemistry, K.Wilson & KH Goulding, ELBS Edition 1986. 4. Essentials of Molecular Biology, David Friefelder, Jones and Barllett Publications, 7th Reprint, 2001. 5. Instant Notes- Biochemistry (1st Indian Edition), B.D. Hames and N.M. Hooper, Viva Books Pvt, Ltd., 2001.

Academic Year: