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Harliansyah, PhD
Head Dept. of Biochemistry
Faculty of Medicine, YARSI University
Objectives
Describe the chemical properties of enzymes:
eg. Active site, catalytic efficiency, specificity, cofactor,
regulation, compartmentalisation.
Explain the classification of enzymes
Describe the kinetics of enzyme catalysis:
-. Michaelis Menten equation
-. Lineweaver Burk transformation
References:
1. Rao, N.M. 2006. Medical Biochemistry. 2nd Ed.
New Age, Publisher.
2. Baynes, J.W. Dominiczak, M.H. 2005. Medical
Biochemistry. 2nd Ed. Elsevier Mosby.
What is Enzyme ?
Catalyst
Increase rate of chemical reactions without changing the equilibrium
Enzymes different from other catalyst:
-. Specific : each enzyme eat different reaction
-. Greater catalytic power than other catalyst
-. Catalytic action can be regulated to ensure rate
of product formed not in excess of amount needed
Localization: organ, tissue, cellular, subcellular
Holoenzyme = Apoenzyme + Cofactor
Reactant = Substrate
Classified in to 6 groups = type of reaction
Active Site
= three dimensional cleft created by side chain of several amino acid
Amino acid from different regions in the linear sequence of enzyme, folded,
side chains close at the active side
Amino acid is classified into 2 functional groups:
1. Binding residues
2. Catalytic residues
Electrostatic
Hydrophobic
Hydrogen Bond
Enzyme Specificity
1. Substrate
2. Reaction
3. Group
4. Absolute group
Reaction Profile
Examples of
Reaction Profile
Examples of
Reaction Profile
Effects of temperature
Effects of pH