06-Discovery of a Substrate Selectivity Switch.pdf

Chemistry Biology 13, 1317–1326, December 2006 ª2006 Elsevier Ltd All rights reserved DOI 10.1016/j.chembiol.2006.10.008 Discovery of a Substrate Selectivity Switch in Tyrosine Ammonia-Lyase, a Member of the Aromatic Amino Acid Lyase Family Kevin T. Watts,1 Benjamin N. Mijts,1 Rhodobacter capsulatus (Integrated Genomics acces- Pyung Cheon Lee,1 Andrew J. Manning,1 sion number: RRC01844) [6], Rba. sphaeroides (Gen- and Claudia Schmidt-Dannert1,2,* Bank accession number: YP_355075) [7], and, very re- 1 Department of Biochemistry, Molecular Biology, cently, Saccharothrix espanaensis (GenBank accession and Biophysics number: ABC88669) [8]. This rarity is likely a reflection University of Minnesota of its specialized role in 4-coumaric acid biosynthesis, 1479 Gortner Avenue which is used as the cofactor for photoactive yellow St. Paul, Minnesota 55108 protein (PYP) in Rhodobacter [9], and initiates the con- version of tyrosine to the N-(m,p -dihydroxycinnamoyl)- taurine moiety of saccharomicin antibiotics [8]. Summary Unique to the aromatic amino acid lyases is the modi- fied amino acid cofactor 3,5-dihydro-5-methylidene-4H- Tyrosine ammonia-lyase (TAL) is a recently described imidazol-4-one (MIO), formed autocatalytically during member of the aromatic amino acid lyase family, which nascent peptide fo