The amino acids from the previous question are both glucogenic and ketogenic. All amino acids will generate urea, and no amino acid is capable of directly interacting with complex 2 of the electron transport chain. That's the job of FAD. So, the answer to this question is all of the above.
Now, the cofactor required for all amino acid degradation pathways is the first transaminase. And in the liver mitochondria, glutamate is converted to alpha-ketoglutarate by a process that can be described as oxidative deamination.
The amino acids serine, cysteine, and alanine are catabolized to yield pyruvate, and these are glucogenic amino acids. Phenylketonuria, which is a genetic disease, can result from the inability to convert phenylalanine, and it's actually the first enzyme in this pathway. A defect in the first enzyme in this pathway that converts phenylalanine to tyrosine. So, babies are checked for certain compounds called phenylacetate, which is just a marker of the inability to convert phenylalanine to tyrosine. If they find phenylacetate in babies, they keep them on a low phenylalanine diet in the early years when their brains are still developing to prevent any problems.
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