Question 5.
KM = (k-1 + k2)/k1, i.e. Higher the Km, the smaller is the binding affinity. Lower the KM, the greater it is.
The slope of the Line-weaver Burk plot = KM/Vmax, KM = slope * Vmax = 1.17 * 4.2 = 4.9 mM
Question 6.
If K-1 >> k2, then KM = k-1/k1 = 1/K, i.e. the reciprocal of the equilibrium constant for the binding of E to S.
Large KM indicates a low affinity of the enzyme for the substrate.
DI LUS his tell you about the T U SHIP Between substrate) and enzymes with high...
biochemistry
if you could please help me answer the following questions!
741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
1. an enzyme is observed to approach an initial velocity of
0.1M/s as more and more [S] is added to the reaction. additionally
when V0 is equal to 0.05 M/s [S] is equal to 0.6 M. based on this
information what is Vmax and Km?
2. If a psrticular enzyme has a Vmax of 0.4 M/s, and a Km of
20 mM, what is V0 wjen [S] = 0.8 M?
3. We have discussed which amino acids chymotrypsin cleaves
at,...
Based on the document below,
1. Describe the hypothesis Chaudhuri et al ids attempting to
evaluate; in other words, what is the goal of this paper? Why is he
writing it?
2. Does the data presented in the paper support the hypothesis
stated in the introduction? Explain.
3.According to Chaudhuri, what is the potential role of thew
alkaline phosphatase in the cleanup of industrial waste.
CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...