BCH210H1 Chapter 20: R20

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

In the previous graphs we were observing low [substrate] concentrations, what would happen as the concentration of substrate is increased: the graph becomes hyperbolic, first order means vo = k[s, it will approach asymptotically known as. Vmax which is maximum velocity of an enzyme: this only occurs when its under saturating conditions (100% of your enzyme saturated, our enzyme won"t work any faster and the vmax will only be dependent on the enzyme concentration. If you double the enzyme concentration under saturated conditions, you"ll double vmax for that particular enzyme reaction. Fundamental equation of enzyme kinematics: louis michaelis and maud menten"s theory, it assumes the formation of an enzyme-substrate complex: K2 is the rate limiting step: it assumes that the es complex is in rapid equilibrium with free enzyme. [es] is constant: breakdown of es to form products is assumed to be slower than, formation of es.