b. From these data compute the value of the \"true\" Vmax and the values of the

Question

b. From these data compute the value of the "true" Vmax and the values of the various Michaelis constants for your mechanism, i.e. Ka, Kb, and Kab.

ii. Does this mechanism fit with the data observed on the previous page for UDP-glucose
pyrophosphorylase and is the binding of the two substrates ordered or random?

3. (6 points) UDP-glucose pyrophosphorylase catalyzes the formation of UDP-glucose, which is the first step in the synthesis of glycogen. Glycogen is the main storage polysaccharide in liver and skeletal muscle (see metabolic pathway handout, p. 1) 20H glucose-1-P UDPG pyrophosphate (PP In order to determine the reaction mechanism of this enzyme, the following steady state kinetic experiments were carried out. UTP KM(ObS)Vmax(obs) Initial velocity (vi) (umoles/mg-min) for glucose-1-P] | [UTP] [UTP] [UTP] = 5.0 uM 5.0 6.7 10.0 15.0 18.2 19.8 20uM 8.3 16.7 25.0 37.5 45.4 49.5 2,000uM 16.7 33.3 50.0 75.0 90.9 99.8 20.0 10 30 100 1000 2000

Explanation / Answer

Based on the given data,

Form this data, the saturation plot is:

So,

a)

The enzyme UDP–glucose pyrophosphorylase form two sets of binary complex reactions, but not a ternary complex.

b)

The data to calculate true Vmax and Km is:

Thus, the LB plot is:

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