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ENZYMOLOGY 2 (BCH 410)
Diagnostic plots for differentiating bisubstrate reactions using steady state method
ENZYMOLOGY 2 (BCH 410)
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MODULE 1 – INTRODUCTION TO ENZYMOLOGY
LEARNING GOALS: To understand the unique properties of enzyme catalysed reactions and also with respect to their active sites and regulatory sites; To be able to identify the active site amino acid groups in an enzyme.
MODULE 2 – MECHANISM OF ACTION OF SOME KNOWNED ENZYMES
LEARNING GOALS: Describe the role of the amino acid residue in the active site of chymotrypsin, ribonuclease A, lysozyme, glutathione reductase and alcohol dehydrogenase. You should also be able to identify and explain the catalytic mechanism of the aforementioned enzymes including pyruvate dehydrogenase complex.
MODULE 3 – MECHANISM AND KINETICS OF BISUBSTRATE REACTIONS
LEARNING GOALS: To be able to differentiate the types of Bisubstrate reactions; To be able to identify & estimate the kinetic parameters (KsA, KmA, KmB and Vmax) from primary and secondary plots for reaction mechanism obeying the general rate equation; To prove that the Alberty rate equation obeys the Michaelis Menten equation; To show the relationship between the Dalzier equation and the Alberty rate equation; To understand how the use of primary plots, product inhibition studies and isotope exchange at equilibrium can be used to diagnose the reaction mechanism employed by a bisubstrate enzyme.
MODULE 4 – TRANSIENT KINETICS, EFFECT OF pH AND TEMPERATURE ON ENZYME ACTIVITY
LEARNING GOALS: To be able to describe the technique used to measure the rates of an enzyme catalysed reaction and to be able to describe and estimate the effect of pH and temperature on enzyme activity.
MODULE 5 – EQUILIBRIUM BINDING EQUATION AND THE SCATCHARD PLOT
LEARNING GOALS: To derive the binding equations for a dimeric and trimeric proteins of identical binding sites, and be able to analyze the equilibrium binding data using the scatchard plot.
LEARNING GOALS: To explain the concept of allosterism and the behaviour of allosteric enzymes using named examples, and also to describe the models of allosterism.
