EC 188.8.131.52 Enzyme
L-tyrosine ammonia-lyase (trans-p-hydroxycinnamate-forming)
L-tyrosine = trans-p-hydroxycinnamate + NH3 [RN:
This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC
(histidine ammonia-lyase), EC
(phenylalanine ammonia-lyase) and EC
(phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family . This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine . The enzyme is far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides [1,2].
EC 184.108.40.206 created 2008 (EC 220.127.116.11 created 1965, part-incorporated 2008)
Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP.
Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.
Chem Biol 13:1327-38 (2006)
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.
Chem Biol 13:1317-26 (2006)
Schwede TF, Retey J, Schulz GE.
Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.
Biochemistry 38:5355-61 (1999)
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