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Tyrosine ammonia-lyase

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Tyrosine ammonia lyase
Identifiers
EC no.4.3.1.23
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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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]

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

See also

References

  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.

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