Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein.
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.
Kyndt
J A
JA
Department of Protein Biochemistry and Protein Engineering, University of Ghent, Ledeganckstraat 35, 9000, Ghent, Belgium.
Meyer
T E
TE
Cusanovich
M A
MA
Van Beeumen
J J
JJ
D000642:Ammonia-Lyases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D003373:Coumaric Acids / Q000378:metabolism*; D020283:Photoreceptors, Microbial / Q000096:biosynthesis; D010860:Pigments, Biological / Q000378:metabolism; D011422:Propionates; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D016354:Rhodobacter capsulatus / Q000201:enzymology* / Q000235:genetics
D001426:Bacterial Proteins; D003373:Coumaric Acids; D020283:Photoreceptors, Microbial; D010860:Pigments, Biological; D011422:Propionates; D011994:Recombinant Proteins; C050162:photoactive yellow protein, Bacteria; D000642:Ammonia-Lyases; C023208:L-tyrosine ammonia-lyase; C495469:p-coumaric acid