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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]

Tyrosine ammonia lyase
Identifiers
EC number4.3.1.23
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
L-Tyrosine   para-coumaric acid + Ammonia + H+

See alsoEdit

ReferencesEdit

  1. ^ 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.
  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. ^ 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.

External linksEdit