This document provides an overview of the topics that will be covered in the Biochemistry course Chem. 433H. The course will focus on biochemical aspects of enzymes, digestion, metabolism of carbohydrates, lipids and proteins, vitamins, and hormones. Specific topics that will be covered include enzymatic kinetics and regulation, digestive processes, glycolysis and the TCA cycle, beta oxidation of fatty acids, amino acid metabolism and the urea cycle, and the structure and function of insulin, thyroxine, and glucocorticoids. Readings from three biochemistry textbooks are suggested.

1. Course No. Chem. 433H ½ Unit, 2 Credit
Topics in Biochemistry 35 + 10 + 5 = 50 Marks
Suggested Readings
1.Biochemistry, Lehninger, Kalyani Publishers.
2.Biochemistry, Styer, W. H. Freeman &
Company.
3.Biochemistry, U. Satyanarayana, New Central
Book Agency (p) Ltd.

2. Course Content
1. Biochemical aspects of Enzymes: Characterization and classification; coenzyme and prosthetic group; chemical
kinetics, michaelis-menten equation, factors affecting the enzymatic reaction, brief treatment on enzymatic reaction
mechanism, substrate specificity of enzymes, catalytic efficiency of enzymes, enzyme inhibition: reversible and
irreversible, regulatory enzymes, allosteric enzymes, covalent modification.
2. Digestive system, digestion and absorption of protein, fat and carbohydrate.
3. Vitamins: Physiological action and sources of vitamin A.D.E.K. and Thiamine, Riboflavin, Niacin, Pantothenic acid,
Folic Acid and Ascorbic acid.
4. Metabolism:
(a) Carbohydrate: Glycolytic pathway: glycolysis and its regulation, feeder pathways,
fate of pyruvate, TCA cycle and its regulation, oxidative phosphorylation,
(b) Lipid: Beta oxidation of even, odd, saturated and unsaturated fatty acid, biosynthesis of fatty
acid.
(c) Protein: Transamination, deamination, decarboxylation, transport of ammonia in the blood
stream, glucose- alanine cycle, urea cycle, link between TCA and urea cycle.
(d) Protein biosynthesis; different types of RNA; simple treatment on protein biosynthesis, genetic
code.
5. Hormones: Classification of hormones, insulin, thyroxine and glucocorticoids: Structure, biochemical aspects and

3. Biochemistry is the branch of science that explores the chemical processes within and
related to living organisms. It is a laboratory based science that brings together biology and
chemistry. By using chemical knowledge and techniques, biochemists can understand and
solve biological problems.
The Chemistry of the living cells
What is Biochemistry?

4. Enzymes
Enzymes are macromolecular biological catalysts that accelerate biochemical reactions.
They are highly specialized protein[exception-RNA acting as ribozyme] having
extraordinary catalytic power(greater than any organic or inorganic catalyst) and high
degree of specificity for their substrate.
Enzyme MW= 12000 to 1 million
Protein Amino acids
Amino acids
2-3 hrs, Enzyme HCl,37C
100 ̊C,Strong acid
2-3 days

5. Enzymes

6.  Isolation of enzyme system from cell-free extract of yeast was achieved in 1883 by
Buchner.
 In 1926 James Sumner first achieved the isolation and crystallization of the enzyme
urease from jack bean and identified it as a protein.
 During this period, J. B. S. Haldane wrote a treatise entitled Enzymes and made the
remarkable suggestion that weak bonding interactions between an enzyme and its
substrate might be used to catalyze a reaction.
 In the 1850s, Louis Pasteur concluded that fermentation of sugar into alcohol
by yeast is catalyzed by "ferments.”
Historical Background Of Enzymes

7. Structure of Enzymes
Cofactors which are small non-protein inorganic molecule that carries out chemical
reactions. Examples of cofactors include metal ions like iron and zinc.
Coenzymes which are organic molecules that are nonproteins and mostly derivatives of
vitamins soluble in water by phosphorylation. Example of coenzyme include thiamine
pyrophosphate (TPP), flavin adenine dinucleotide (FAD), biotin

8. Apoenzyme is an inactive form of enzyme lacking the association of coenzyme and/or
cofactors. Activation of the enzyme occurs upon binding of an organic or inorganic
cofactor.
Holoenzyme is a complete and catalytically active form of enzyme. An apoenzyme
together with its cofactor is holoenzyme. Examples of holoenzymes include DNA
polymerase and RNA polymerase which contain multiple protein subunits
The active site of an enzyme represents as the small region at which the substrates binds
and participates in the catalysis.
Structure of Enzymes

9. The term prosthetic group is used when the non-protein moiety tightly (covalently) binds
with the apoenzyme. The coenzyme can be separated by dialysis from the enzyme while the
prosthetic group cannot be.
Structure of Enzymes