enzyme kinetics Flashcards
The region of an enzyme which binds to its substrate is called the ……
Where the shape of an enzymes active site and substrate are very similar, they can be said to be Blank 1 in shape, in this case the enzyme:substrate binding could be described by the Blank 2 and Blank 3 theory. Where the two are not perfectly complementary, the enzyme may undergo a Blank 4 change upon substrate binding, this is described by the Blank 5 - Blank 6 theory of enzyme:substrate binding.
Overall, the presence of an enzyme will mean more of the product of a reaction is produced by shifting the equilibrium position to favour products true/false
A graph plotted of rate of reaction against substrate concentration for an enzyme displaying typical Michaelis Menten kinetics could be described as what shape?
For a typical Michaelis Menten enzyme, the concentration of substrate that gives a rate of reaction equal to half the maximum rate is called what?
In an enzyme catalysed reaction, displaying Michaelis Menten kinetics, the pressence of an inhibitor leads to an increase in the observed Km, though the Vmax does not change. What type of inhibition is this?
The glucokinase enzyme, found mainly in the liver is highly specific for glucose as its substrate, unlike other hexokinases. However, the Km of glucokinase with glucose as the substrate is around 100X higher than hexokinase (10mM compared to 0.1mM). Why would there be such a high Km and apparent lower affinity of glucokinase for its substrate and how could this relate to its physiological role?
How is the paramater Kcat derived and what does this tell us?
Another important parameter is the value given by Kcat/Km what does this tell us?
If you were wanting to plot a graph of rate vs. substrate concentration in the pressence and absence of an inhibitor, which type of plot (Michaelis Menten OR Lineweaver-Burk) would be more accurate to use in order to determine the type of inhibition? Explain your answer.
