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For example, are there pathways for the deamination of phenylalanine that simply produce ammonia or pathways for it to be synthesized from phenylpyruvate with ammonia being utilized to form the amine group?

Preferably, I want to know how it is with human metabolism mainly.

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    $\begingroup$ What research of your own have you done to answer this question? Amino acid synthesis and degradation are covered on numerous internet sites and in texts on NCBI Bookshelf. Please consult the Help on asking good questions to find out what is expected from posters of questions. (And also include the question in the main body so that it is complete in itself.) $\endgroup$ – David Oct 4 '19 at 22:05
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    $\begingroup$ I'm not going to give you the answer, but Berg et al. Biochemistry on NCBI Bookshelf is a good starting point for any biochemical questions. Search for deamination and read the whole section. Tell us what you find — you could even make it an answer to help others and get yourself some credit. $\endgroup$ – David Oct 6 '19 at 21:41
  • $\begingroup$ thanks, I will! $\endgroup$ – Dahen Oct 8 '19 at 18:35
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For most amino acids, the removal of the α-amino group involves α-ketoglutarate and glutamate. The amino group is first transferred to a-ketoglutarate by transaminases, and the resulting glutamate is then deaminated (via glutamate dehydrogenase) to yield ammonia. enter image description here

The same is true for amination. Glutamate and glutamine are the two major amino group-donors. Most ketoacids are converted to their respective amino acids by transamination involving glutamate or glutamine. Glutamine can be synthesized by amination of glutamate with ammonia without transamination (via a synthetase enzyme) and glutamate can be aminated with ammonia too.

Exceptions do exist, of course. For example, Not all transaminations involve glutamate/glutamine (as this user has replied), and serine and threonine can be directly deaminated (via dehydratase enzymes, as opposed to the dehydrogenase used for glutamate).

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