Fenilalaninska amonijak-lijaza

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Fenilalaninska amonijak-lijaza
Phenylalanine ammonia lysase active site.png
EC broj
CAS broj 9024-28-6
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures

Fenilalaninska amonijak-lijaza (EC, fenilalaninska deaminaza, fenilalaninska amonijum-lijaza, PAL, L-fenilalaninska amonijak-lijaza, Phe amonijak-lijaza) je enzim sa sistematskim imenom L-fenilalanin amonijak-lijaza (formira trans-cinamat).[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-fenilalanin trans-cinamat + NH3

Ovaj enzim je član familije lijaza aromatičnih aminokiselina.


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


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