EC 4.3.1.24 - Phenylalanine ammonia-lyase

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IntEnz Enzyme Nomenclature
EC 4.3.1.24

Names

Accepted name:
phenylalanine ammonia-lyase
Other names:
PAL
phenylalanine ammonium-lyase
phenylalanine deaminase
L-phenylalanine ammonia-lyase
Phe ammonia-lyase
Systematic name:
L-phenylalanine ammonia-lyase (trans-cinnamate-forming)

Reaction

Cofactor

Comments:

This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase) and EC 4.3.1.23 (tyrosine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [3]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [9]. The enzyme from some species is highly specific for phenylalanine [7,8].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00424
Structural data: CSA , EC2PDB
Gene Ontology: GO:0045548
CAS Registry Number: 9024-28-6
UniProtKB/Swiss-Prot: (56) [show] [UniProt]

References

  1. Koukol, J. and Conn, E.E.
    The metabolism of aromatic compounds in higher plants. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare.
    J. Biol. Chem. 236: 2692-2698 (1961). [PMID: 14458851]
  2. Young, M.R. and Neish, A.C.
    Properties of the ammonia-lyases deaminating phenylalanine and related compounds in Triticum sestivum and Pteridium aquilinum.
    Phytochemistry 5: 1121-1132 (1966).
  3. Louie, G.V., Bowman, M.E., Moffitt, M.C., Baiga, T.J., Moore, B.S., and Noel, J.P.
    Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.
    Chem. Biol. 13: 1327-1338 (2006). [PMID: 17185228]
  4. Calabrese, J.C., Jordan, D.B., Boodhoo, A., Sariaslani, S., and Vannelli, T.
    Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis.
    Biochemistry 43: 11403-11416 (2004). [PMID: 15350127]
  5. Ritter, H. and Schulz, G.E.
    Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase.
    Plant Cell 16: 3426-3436 (2004). [PMID: 15548745]
  6. Watts, K.T., Mijts, B.N., Lee, P.C., Manning, A.J. and Schmidt-Dannert, C.
    Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family.
    Chem. Biol. 13: 1317-1326 (2006). [PMID: 17185227]
  7. Appert, C., Logemann, E., Hahlbrock, K., Schmid, J. and Amrhein, N.
    Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley (Petroselinum crispum Nym.).
    Eur. J. Biochem. 225: 491-499 (1994). [PMID: 7925471]
  8. Cochrane, F.C., Davin, L.B. and Lewis, N.G.
    The Arabidopsis phenylalanine ammonia lyase gene family: kinetic characterization of the four PAL isoforms.
    Phytochemistry 65: 1557-1564 (2004). [PMID: 15276452]
  9. Schwede, T.F., Rétey, J. and Schulz, G.E.
    Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.
    Biochemistry 38: 5355-5361 (1999). [PMID: 10220322]

[EC 4.3.1.24 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)]