Primary Structure - Proteins

Example: A change in the amino acid sequence leads to Sickle Cell Anemia
 Secondary structure – Protein
example for error: Mad cow/Creutzfeld-Jacobs Disease
Tertiary structure: Water-soluble proteins fold
into compact structures with non-polar cores
Myoglobin

Yellow: hydrophobic amino acids

Blue: charged amino acids
White: white: others
 Some proteins fold into domains
quarternary structure

Extracellular part of CD4, cell surface protein on immuno

cells that is essential for HIV-infection –
four similar domains of 100 aa
What are enzymes?
 Enzymes are powerful and highly
specific catalysts of cellular reactions

l Enzymes accelerate reactions by

factors of as much as a million or more
Carbonic anhydrase
Enzyme (E)

Substrates (S) Products (P)

Hydration of CO2 by carbonic anhydrase: 106 molecules per second

107 times faster than uncatalyzed
 Enzymes are highly specific
l Enzymes are highly specific in catalysing
a single chemical reaction or a set of
closely related reactions in transforming
substrates

Trypsin

l Specificity is due to
precise interaction
of substrate with
enzyme at active site
Precision is Thrombin
a result of 3-
dimensional structure
of the enzyme
Models of Enzyme/Substrate binding sites:
lock-and-key

This model presumes that there is a perfect fit between the substrate and the active site –
the two molecules are complementary in shape. Lock-and-key is the model such that
active site of enzyme is good fit for substrate that does not require
change of structure of enzyme after enzyme binds substrate
Models of Enzyme/Substrate binding sites:
Induced-fit
Enzymes accelerate reactions by facilitating
the formation of a transition state

Enzyme/Substrate complex

S+E ES P+E

Formation of product
or decrease of substrate
can be measured
Model of enzyme active site - Trypsin
Many enzymes need co-factors – Example: Succinate dehydrogenase

Co-factors are
non-protein molecules

Without co-factors the

active site of an enzyme
is not active

FADH2
Iron/sulphur centers
for e-transfer

Heme
Enzymes are classified on the basis of
the types of reactions they catalyse
Table 8.3. Six major classes of enzymes

Class Type of reaction Example Cha

1. Oxidation-reduction Lactate dehydrogenase

Oxidoreductases
2. Transferases Group transfer Nucleoside monophosphate
kinase (NMP kinase)
3. Hydrolases Hydrolysis reactions (transfer of Chymotrypsin
functional groups to water)
4. Lyases Addition or removal of groups to Fumarase
form double bonds
5. Isomerases Isomerization (intramolecular Triose phosphate isomerase
group transfer)
6. Ligases Ligation of two substrates at the Aminoacyl-tRNA synthetase
expense of ATP hydrolysis