Phenylalanine/tyrosine ammonia-lyase

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Phenylalanine/tyrosine ammonia-lyase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Phenylalanine/tyrosine ammonia-lyase (EC, PTAL, bifunctional PAL) is an enzyme with systematic name L-phenylalanine(or L-tyrosine):trans-cinnamate(or trans-p-hydroxycinnamate) ammonia-lyase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

(1) L-phenylalanine trans-cinnamate + NH3
(2) L-tyrosine trans-p-hydroxycinnamate + NH3

This enzyme is a member of the aromatic amino acid lyase family.


  1. ^ Rösler, J.; Krekel, F.; Amrhein, N.; Schmid, J. (1997). "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity". Plant Physiol. 113: 175–179. PMC 158128Freely accessible. PMID 9008393. doi:10.1104/pp.113.1.175. 
  2. ^ Watts, K.T.; Mijts, B.N.; Lee, P.C.; Manning, A.J.; 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. doi:10.1016/j.chembiol.2006.10.008. 
  3. ^ Louie, G.V.; Bowman, M.E.; Moffitt, M.C.; Baiga, T.J.; Moore, B.S.; Noel, J.P. (2006). "Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases". Chem. Biol. 13: 1327–1338. PMC 2859959Freely accessible. PMID 17185228. doi:10.1016/j.chembiol.2006.11.011. 
  4. ^ Schwede, T.F.; Rétey, J.; 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. doi:10.1021/bi982929q. 
  5. ^ Barros, J.; Serrani-Yarce, J.C.; Chen, F.; Baxter, D.; Venables, B.J.; Dixon, R.A. (2016). "Role of bifunctional ammonia-lyase in grass cell wall biosynthesis". Nat. Plants. 2: 16050. PMID 27255834. doi:10.1038/nplants.2016.50. 

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