BCHS316

Enzymology
Dr Matsobane Tlou
(Office: A4-1018)
Why studying Enzymology as a
full module on 3 year level!?
rd
Applications (Ch. 19 and 20 in text book)

Medicine
Diagnostics (plasma enzymes)
Reagents in clinical chemistry
Pharmaceutical industry

Biotechnology
Food industry
Agriculture
Science and technology

Other reasons?
 Outcomes
After completing the study unit you should have
knowledge of the following aspects:

• A historical overview of the study of enzymes;

• The classification of enzymes;
• The structural aspects of enzymes;
• The structure-function relation of monomeric
and oligomeric enzymes.
 Content
1.1 Introduction to Enzymology (Ch. 1)
1.2 The structure of proteins (Ch. 2 and 3)
1.3 The specificity of enzyme function (Ch. 4)
1.4 Monomeric and oligomeric enzymes (Ch. 5)
 LE / SU 1
Enzymes?

apoenzyme
coenzyme
+ cofactor prosthetic group
metal ion
= holoenzyme

Isoenzymes
 History
• 1833 – partial isolation of diastase (amylase)
• Justus von Liebig – non-living material
Louis Pasteur – living material
• 1878 – ferments to enzymes (Wilhelm Kühne)
• 1897 – Eduard and Hans Büchner
• 1926 – James Sumner crystallises urease from
jack-bean extracts
• Many other enzymes purified and crystallised
 Naming and classification
• Enzymes end with –ase (amylase)
but proteolytic enzymes end with –in (trypsin)
• Confusion follows
• IUBMB appoints commission
• Enzyme commission divides enzymes into 6
main classes, appoints 4 digit code (E.C. 1.4.2.2)
plus a systemic name
 Classification
First digit Enzyme class Type of reaction catalysed

1 Oxidoreductases Oxidation/ Reduction reactions

2 Tranferases Transfer of an atom or group between two

molecules (excluding reaction in other classes)
3 Hydrolases Hydrolysis reactions

4 Lyases Removal of a group by a substrate

(not by hydrolyses)
5 Isomerase Isomerisation reactions

6 Ligases Synthetic joining of two molecules using ATP

 Protein Structure
• Primary structure: amino acid sequence
• Secondary structure: local substructures
(alpha helix and beta strands)
• Tertiary structure: 3D structure of single
protein molecule
• Quaternary structure: assembly of several
protein molecules
 Specificity of enzyme action
• Group specificity: hexokinase

• Absolute specificity: glucokinase

• Product and substrate specific

• Stereochemical specificity
 Specificity of enzyme action
Enzymes contain active sites:
• binding site
• catalytic site
 Fischer ‘lock-and-key’ hypothesis

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are
 Koshland ‘induced fit’ hypothesis

• Strain and transition-state stabilisation

 Monomeric and oligomeric
enzymes
• Monomeric enzymes: single polypeptide
chain, very few known, all catalyse hydrolytic
reactions
– Ex: trypsin
• Oligomeric enzymes: two or more polypeptide
chains, consists of sub-units, almost all
enzymes are oligomeric
– Ex: lactate dehydrogenase (LDH)
 Vi

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