Again I am studying for a biochemistry test and as anyone reading this would notice the exam is this week and I am using my 30 minutes of daily writing to help me dive in to concepts with words rather than images or equations. There is many ways to express the activity of enzymes and one way is with the rules that Michaelis and Menten have laid out. They make three assumptions. The first being that there is no k-2. This means that any amount of enzyme product complex is negligible so it isn’t counted, it also means that free enzymes and products will never complete a reverse reaction to return to the enzyme substrate complex. The second assumption is that the concentration of the enzyme substrate complex remains constant when measuring the initial velocity. The third assumption is that Vmax can always be reached, this means that you can always react the most available enzymes with the most available substrates. Putting all of these assumptions together you can fully understand the equation. E+S<->ES<->E+P. E is enzyme, S is substrate, P is product, ES is enzyme substrate complex. You can go back and forth between the free enzymes and free substrates state and the enzyme substrate complex. The rate at which the enzyme substrate complex is formed remains constant. Once you pass the enzyme substrate complex to the free enzyme and product you can no longer return to the enzyme substrate complex. When graphed you can always relate the substrate concentration to the velocity. This is where you can derive the relation Km=[substrate] at ½ Vmax.
Recent comments