- Information
- AI Chat
Lecture 23 Enzyme Kinetics 1
Biomolecules
University of Lincoln
Preview text
Enzyme Kinetics
● Principles of enzymatic catalysis ○ Gibbs free energy (ΔG) is the difference between the free energy of the products (P) and that of the reactants/substrate (S) ○ Enzymes speed up the rate of reactions by lowering the activation energy - needed to start the reaction - enzymes speed up the reaction by lowering the activation energy ○ Enzymes are not consumed in the reaction ○ Enzymes do not change the equilibrium, as ΔG remains the same - because the energy levels of the substrates are still exactly the same
● Why study enzyme kinetics? ○ To determine catalytic efficiency and rates of the enzyme reaction ○ To determine binding constants for substrates and inhibitors (e. drugs that are commercially available may be enzyme inhibitors for the reaction) ○ To elucidate reaction mechanisms (number of steps, nature of intermediates etc) - studying the mechanism will tell you a lot about the enzyme ○ To understand metabolic pathways - biochemical pathways
○ To determine enzyme concentrations (clinical diagnostics) - e. enzyme called ALT - knowing the amount of the enzyme in the body can tell you the potential hepatocellular damage or forms of hepatitis ○ Alanine aminotransferase (ALT): ■ Hepatocellular damage ■ Hepatitis B and C
● Reaction rates
● reaction as a 1st order rate - can be described as 'K' - when happens at 320 degrees, K = 2 x 10 ^-5 s-1 - rate is very small ● K is the rate of conversion ● when there is a smaller concentration - it will have the same rate just at a lower point on the y axis ● the concentration of the SO2Cl2 will be the same when the compounds are separated - so SO2 and Cl2 will have the same concentration as there is only one of each compound ● the tangent of the reaction is the curve ● v = velocity
Lecture 23 Enzyme Kinetics 1
Module: Biomolecules
University: University of Lincoln
- More from:BiomoleculesUniversity of Lincoln33 Documents
