show all work plz Question 9 You are studying glycolysis in a cell free extract
ID: 62195 • Letter: S
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show all work plz
Question 9 You are studying glycolysis in a cell free extract of muscle and you find that, in an oxygen-free atmosphere, the extract efficiently converts glucose to lactate. You then do an experiment in which you add an inhibitor, oxamate, to the extract in addition to glucose. You find that fructose-1,6-bisphosphate, dihydroxyacetone phosphate and glyceraldehyde-3-phosphate accumulate to high concentrations, while 1,3-bisphosphoglycerate, phosphoenolpyruvate and pyruvate are at very low concentrations. (a) Basest on the result of this experiment, what enzyme do you think is inhibited by oxamate? You now repeat the experiment, but you add a high concentration of NADI to the extract in addition to glucose and oxamate. Now, pyruvate accumulates in the cell extract, but no other intermediates of glycolysis accumulate, and lactate is undetectable. (b) Based on this new evidence, what do you now think is the target for inhibition by oxamate? What is your revised explanation for the result of the first experiment?Explanation / Answer
SOLUTION:
A: Enzyme LDH is inhibited by oxamate.
Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. LDH is a key enzyme in anaerobic respiration. Anaerobic Respiration is the conversion of pyruvate into lactate acid in the absence oxygen. This pathway is important to glycolysis in two main ways. The first is that if pyruvates were to build up glycoysis and thus the generation of ATP would slow. The second is anaerobic respiration allows for the regeneration of NAD+ from NADH. NAD+ is required when glyceraldehyde-3-phosphate dehydrogenase oxidizes glyceraldehyde-3-phosphate in glycolysis, which generates NADH. Lactate dehydrogenase is responsible for the anaerobic conversion of NADH to NAD+.
B: Pyruvate kinase is enzyme inhibited in second experiment.
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