Phenylalanine ammonia-lyase

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In enzymology, a phenylalanine ammonia-lyase (EC 4.3.1.5) is an enzyme that catalyzes the chemical reaction

L-phenylalanine trans-cinnamate + NH3

Hence, this enzyme has one substrate, L-phenylalanine, and two products, trans-cinnamate and NH3.

This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-phenylalanine ammonia-lyase (trans-cinnamate-forming). Other names in common use include tyrase, phenylalanine deaminase, tyrosine ammonia-lyase, L-tyrosine ammonia-lyase, phenylalanine ammonium-lyase, PAL, and L-phenylalanine ammonia-lyase. This enzyme participates in 5 metabolic pathways: tyrosine metabolism, phenylalanine metabolism, nitrogen metabolism, phenylpropanoid biosynthesis, and alkaloid biosynthesis ii.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1T6J, 1T6P, 1W27, 1Y2M, and 2NYF.

References

  • IUBMB entry for 4.3.1.5
  • BRENDA references for 4.3.1.5 (Recommended.)
  • PubMed references for 4.3.1.5
  • PubMed Central references for 4.3.1.5
  • Google Scholar references for 4.3.1.5
  • KOUKOL J, CONN EE (1961). "The metabolism of aromatic compounds in higher plans. IV Purification and properties of the phenylalanine deaminase of Hordeum vulgare". J. Biol. Chem. 236: 2692&ndash, 8. PMID 14458851.
  • Young MR and Neish AC (1966). "Properties of the ammonia-lyases deaminating phenylalanine and related compounds in Triticum sestivum and Pteridium aquilinum". Phytochemistry. 5: 1121&ndash, 1132.

External links

The CAS registry number for this enzyme class is 9024-28-6.

Gene Ontology (GO) codes


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