Phenylalanine/tyrosine ammonia-lyase
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EC no.4.3.1.25
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Phenylalanine/tyrosine ammonia-lyase (EC 4.3.1.25, 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.

References

  1. ^ Rösler J, Krekel F, Amrhein N, Schmid J (January 1997). "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity". Plant Physiology. 113 (1): 175–9. doi:10.1104/pp.113.1.175. PMC 158128. PMID 9008393.
  2. ^ Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C (December 2006). "Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family". Chemistry & Biology. 13 (12): 1317–26. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227.
  3. ^ Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP (December 2006). "Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases". Chemistry & Biology. 13 (12): 1327–38. doi:10.1016/j.chembiol.2006.11.011. PMC 2859959. PMID 17185228.
  4. ^ Schwede TF, Rétey J, Schulz GE (April 1999). "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile". Biochemistry. 38 (17): 5355–61. doi:10.1021/bi982929q. PMID 10220322.
  5. ^ Barros J, Serrani-Yarce JC, Chen F, Baxter D, Venables BJ, Dixon RA (May 2016). "Role of bifunctional ammonia-lyase in grass cell wall biosynthesis". Nature Plants. 2 (6): 16050. doi:10.1038/nplants.2016.50. PMID 27255834.

External links

Carbon–nitrogen lyases (EC 4.3)
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