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MetNet - plant pathway - phenylalanine degradation III
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Pathway details: phenylalanine degradation III


General info Interaction details Linked pathways Protein-protein interactions
Notes
  Pathway was created on Mon Jul 29, 2013.
 Contributed by aracyc:
While can utilize only a limited range of carbon sources it can obtain its nitrogen from many different sources, including most amino acids |CITS: [Large 68]|. The most common mechanism for retrieving the nitrogen from amino acids is transamination, using α-ketoglutarate or other 2-oxo acids as amino acceptors. This process leaves the carbon skeleton of the amino acid intact, in the form of a 2-oxo acid. In a few cases the resulting 2-oxo acid can be directly fed into central metabolism (such as the case of L-alanine and its derived 2-keto acid, pyruvate). In most cases, though, the 2-oxo acids resulting from transamination are not intermediates of central metabolism, and are excreted from the cells after some transformation. An important and common pathway for catabolism of amino acids by yeast is the Ehrlich pathway |CITS: [Ehrlich07]|. In this pathway, following transamination of an amino acid into the corresponding 2-oxo acid, the 2-oxo acid is decarboxylated to an aldehyde. Depending on the redox status of the cells , the aldehydes can then be either reduced (by alcohol dehydrogenases) to alcohols, which are called collectively "fusel alcohols", or oxidized by aldehyde dehydrogenases to organic acids (?fusel acids?) . Aromatic amino acids, such as L-phenylalanine, can be used as a nitrogen source, but not as a carbon source. Following the transamination of L-phenylalanine to phenylpyruvate, the 2-oxo acid is converted to phenylacetaldehyde and eventually 2-phenylethanol, which is excreted from the cell . The first step is performed by either of two aromatic amino acid transaminases. is the main catabolic enzyme, and accepts phenylpyruvate, pyruvate or p-hydroxyphenylpyruvate, but not α-ketoglutarate, as the amino acceptor . However, a reaction utilizing α-ketoglutarate as the amino acceptor has also been demonstrated, and is likely catalyzed by . Once transaminated, the 2-oxo acid is decarboxylated by either of four decarboxylases, although recent results suggest that the main decarboxylase performing this reaction in vivo is the encoded by the gene , whose expression increased 30-fold when L-phenylalanine replaced ammonia as the culture's nitrogen source . The last step of this pathway can be performed by any of the yeast alcohol dehydrogenases .
  Parts of this pathway occur in:   cytosol     nucleus     endoplasmic reticulum  


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metabolite [13]
protein complex [4]
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