In the TCA cycle what is the structure and function of thiamine, nicotinamide enzymes, Flavin, coenzyme A, and lipoic acid in both reduced and oxidized state if possible?

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Tod ThielLv2

23 Oct 2019

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64. For the pyruvate dehydrogenase complex, what is the specific chemical function of the thiamine pyrophosphate cofactor?

A. activation of acetyl-CoA

B. oxidation of lipoic acid

C. reduction of NAD+D. transfer of the acetyl group to CoA

E. decarboxylation of pyruvate

2. which of the following co factors would be required to transfer a carboxyl group onto pyruvate to form oxaloacetate?

a. thiamine pyrophosate

b. tetrahydrofolate

c. ascorbic acid

d. cobalamin

e. biotin

Pyruvate dehydrogenase is a large, highly integrated complex containing many copies of three distinct enzymes. There are five coenzymes involved in its catalytic activity: NAD , FAD, coenzyme A, lipoamide, and thiamine pyrophosphate (TPP or TDP). The coenzymes can be classified depending on how they participate in an enzymatic reaction.

A coenzyme prosthetic group is tightly bound to the enzyme and remains bound during the catalytic cycle.

The original coenzymes are regenerated during the catalytic cycle.

On the other hand, a coenzyme cosubstrate is loosely bound to an enzyme and dissociates in an altered form as part of the catalytic cycle. Its original form is regenerated not by the cycle, but by another enzyme.