Biology, asked by amyblessy7850, 11 months ago

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.

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Answered by larus
3

Thiamine pyrophosphate, FAD, and lipoamide are the coenzyme prosthetics.  

Prosthetic gatherings refer to the cofactors, which attaches resolutely with the catalysts or proteins. They can be particles of metal or are natural, and are frequently joined with the proteins by a covalent bond.  

The similar cofactors can attach with numerous different kinds of proteins and may combine with a few compounds freely, as a coenzyme, and with others firmly as a prosthetic gathering. Some of the cofactors can consistently resolutely attach with their chemicals. However, it is essential to note that these prosthetic gatherings can similarly combine with proteins other than the catalysts.  


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