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
| Phenylalanine/tyrosine ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.25 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- (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
edit- ^ 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 9008393.175-9&rft.date=1997-01&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC158128#id-name=PMC&rft_id=info:pmid/9008393&rft_id=info:doi/10.1104/pp.113.1.175&rft.aulast=Rösler&rft.aufirst=J&rft.au=Krekel, F&rft.au=Amrhein, N&rft.au=Schmid, J&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC158128&rfr_id=info:sid/en.wikipedia.org:Phenylalanine/tyrosine ammonia-lyase" class="Z3988">
- ^ 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 17185227.1317-26&rft.date=2006-12&rft_id=info:doi/10.1016/j.chembiol.2006.10.008&rft_id=info:pmid/17185227&rft.aulast=Watts&rft.aufirst=KT&rft.au=Mijts, BN&rft.au=Lee, PC&rft.au=Manning, AJ&rft.au=Schmidt-Dannert, C&rfr_id=info:sid/en.wikipedia.org:Phenylalanine/tyrosine ammonia-lyase" class="Z3988">
- ^ 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 17185228.1327-38&rft.date=2006-12&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2859959#id-name=PMC&rft_id=info:pmid/17185228&rft_id=info:doi/10.1016/j.chembiol.2006.11.011&rft.aulast=Louie&rft.aufirst=GV&rft.au=Bowman, ME&rft.au=Moffitt, MC&rft.au=Baiga, TJ&rft.au=Moore, BS&rft.au=Noel, JP&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2859959&rfr_id=info:sid/en.wikipedia.org:Phenylalanine/tyrosine ammonia-lyase" class="Z3988">
- ^ 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 10220322.5355-61&rft.date=1999-04&rft_id=info:doi/10.1021/bi982929q&rft_id=info:pmid/10220322&rft.aulast=Schwede&rft.aufirst=TF&rft.au=Rétey, J&rft.au=Schulz, GE&rfr_id=info:sid/en.wikipedia.org:Phenylalanine/tyrosine ammonia-lyase" class="Z3988">
- ^ 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
edit- Phenylalanine/tyrosine ammonia-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
