Tyrosine ammonia-lyase explained
Tyrosine ammonia lyase |
Ec Number: | 4.3.1.23 |
Tyrosine ammonia lyase (EC 4.3.1.23, 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]
+
Ammonia + H
+L-tyrosine =
trans-p-hydroxycinnamate + NH
3See also
External links
Notes and References
- Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP . Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases . Chemistry & Biology . 13 . 12 . 1327–38 . December 2006 . 17185228 . 2859959 . 10.1016/j.chembiol.2006.11.011 .
- Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C . 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 . December 2006 . 17185227 . 10.1016/j.chembiol.2006.10.008 .
- Schwede TF, Rétey J, Schulz GE . Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile . Biochemistry . 38 . 17 . 5355–61 . April 1999 . 10220322 . 10.1021/bi982929q .