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

FEBS Letters

Van Beeumen, J.J.¹  Kyndt, J.A.¹  Cusanovich, M.A.²  Meyer, T.E.² 

[1] Department of Protein Biochemistry and Protein Engineering, University of Ghent, Ledeganckstraat 35, 9000 Ghent, Belgium;Department of Biochemistry, University of Arizona, 1041 E. Lowell St., Tucson, AZ 85721, USA

关键词: Tyrosine ammonia lyase;    Photoactive yellow protein;    p-Hydroxycinnamic acid;    Phenylalanine ammonia lyase;    Rhodobacter capsulatus;    ORF;    open reading frame;    TAL;    tyrosine ammonia lyase;    PAL;    phenylalanine ammonia lyase;    HAL;    histidine ammonia lyase;    PYP;    photoactive yellow protein;    K m;    Michaëlis–Menten constant;    k cat;    turnover number;    pCL;    p-coumaryl:coenzyme A ligase;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/S0014-5793(02)02272-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown