Phenylalanine/tyrosine ammonia-lyase

Phenylalanine/tyrosine ammonia-lyase
Identifiers
EC number	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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ trans-cinnamate + NH₃

(2) L-tyrosine $\rightleftharpoons$ trans-p-hydroxycinnamate + NH₃

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

References

1. Rösler, J., Krekel, F., Amrhein, N. and 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.
2. 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. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227.
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. doi:10.1016/j.chembiol.2006.11.011. PMID 17185228.
4. 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. doi:10.1021/bi982929q. PMID 10220322.

External links

• Phenylalanine/tyrosine ammonia-lyase at the US National Library of Medicine Medical Subject Headings (MeSH)