) In the presence of FBP, you find that BLLDH goes from-9 to ~91% pyruvate-bound
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Question
) In the presence of FBP, you find that BLLDH goes from-9 to ~91% pyruvate-bound over a-2 fold concentration range of the substrate. You come across a new mutant of BLLDH that eliminates allosteric communication between subunits but retains the rather high affinity Ko of the native protein for pyruvate of 1 M. ew mutant. Draw in the expected binding curves below for the native enzyme and yourn Explain your logic below. 16 pts) i. native mutant 0 10 0.1 10 0 0.1 [pyruvate] uM [pyruvate] uM CL) ii. What consequence does the mutation have for production of lactate over the concentration range of substrate depicted above? Explain your logic. (4 pts)Explanation / Answer
A)
The native had a sigmoidal saturation curve for pyruvate even in the presence of FBP. This property can be accounted by the presence of functional FBP-binding sites.
The mutant had desensitized to FBP , so they had no intact FBP-binding sites in presence of high affinity of native protein. Native had a sigmoidal saturation curve for pyruvate even in the presence of FBP. This property can be accounted by the presence of functional FBP-binding sites.
B)
In Mutant , there are no active binding site for substrate in enzyme, so which had no catalytic activity. there are no lactate production had occured.
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