Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein

• Published in: FEBS letters 2002-02, Vol.512 (1), p.240-244
• Main Authors: Kyndt, J.A., Meyer, T.E., Cusanovich, M.A., Van Beeumen, J.J.
• Format: Article
• Language: English
• Subjects: Ammonia-Lyases - genetics; Ammonia-Lyases - isolation & purification; Ammonia-Lyases - metabolism; Bacterial Proteins - biosynthesis; Bacterial Proteins - genetics; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Coumaric Acids - metabolism; HAL, histidine ammonia lyase; k cat, turnover number; K m, Michaëlis–Menten constant; ORF, open reading frame; p-Hydroxycinnamic acid; PAL, phenylalanine ammonia lyase; pCL, p-coumaryl:coenzyme A ligase; Phenylalanine ammonia lyase; Photoactive yellow protein; Photoreceptors, Microbial - biosynthesis; Pigments, Biological - metabolism; Propionates; PYP, photoactive yellow protein; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Rhodobacter capsulatus; Rhodobacter capsulatus - enzymology; Rhodobacter capsulatus - genetics; TAL, tyrosine ammonia lyase; TFA, trifluoroacetic acid; Tyrosine ammonia lyase
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(02)02272-X

During genome sequence analysis of Rhodobacter capsulatus, nearby open reading frames were found that encode a photoactive yellow protein (PYP) and a hypothetical biosynthetic enzyme for its chromophore, a tyrosine ammonia lyase (TAL). We isolated the TAL gene, overproduced the recombinant protein in Escherichia coli, and after purification analyzed the enzyme for its activity. The catalytic efficiency for tyrosine was shown to be approximately 150 times larger than for phenylalanine, suggesting that the enzyme could in fact be involved in biosynthesis of the PYP chromophore. To our knowledge it is the first time this type of enzyme has been found in bacteria.