Phenylalanine/tyrosine ammonia-lyase
| 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 | ||||||||
| |||||||||
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] 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
- ^ Rösler, J.; Krekel, F.; Amrhein, N.; Schmid, J. (1997). "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity". Plant Physiol. 113: 175–179. doi:10.1104/pp.113.1.175. PMID 9008393.
- ^ 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. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227.
- ^ 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. doi:10.1016/j.chembiol.2006.11.011. PMID 17185228.
- ^ 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. doi:10.1021/bi982929q. PMID 10220322.
External links
- Phenylalanine/tyrosine+ammonia-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)