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Describe howα-ketoglutarate and oxaloacetate participate in amino acid catabolism.

Short Answer

Expert verified

Transamination, which involves transferring an amino group from a -keto acid to a new amino acid, is the process used to deaminate amino acids. The primary amino group acceptor, -ketoglutarate, yields glutamate and the newly discovered -keto acid.

Step by step solution

01

Aminotransferase catalytic cycle.  

The coenzyme has to be changed from PMP back to the enzyme-PLP Schiff base in order to finish the catalytic cycle of the aminotransferase. As a result, amino groups from amino acids that engage in transamination events with -ketoglutarate are removed by the glutamate dehydrogenase process.

02

Production of α-keto acid. 

The coenzyme has to be changed from PMP back to the enzyme-PLP Schiff base in order to finish the catalytic cycle of the aminotransferase. As a result, amino groups from amino acids that engage in transamination events with -ketoglutarate are removed by the glutamate dehydrogenase process.

03

Production of oxaloacetate.  

In a subsequent transamination event, the amino group of glutamate can be transferred to oxaloacetate, producing aspartate and regenerating -ketoglutarate. Hydrolysis of the -keto acid-PMP Schiff base yields PMP and a -keto acid.

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