Tyrosine ammonia-lyase

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Tyrosine ammonia lyase
Identifiers
EC number 4.3.1.23
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Tyrosine ammonia lyase (L-tyrosine ammonia-lyase, TAL or Tyrase) is an enzyme in the natural phenols biosynthesis pathway. It transforms L-tyrosine into p-coumaric acid.[1][2][3]

L-Tyrosine   para-coumaric acid + Ammonia + H+

See also[edit]

References[edit]

  1. ^ 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. 
  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. doi:10.1016/j.chembiol.2006.10.008. PMID 17185227. 
  3. ^ 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[edit]