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

被引:147
作者
Kyndt, JA
Meyer, TE
Cusanovich, MA
Van Beeumen, JJ
机构
[1] State Univ Ghent, Dept Prot Biochem & Prot Engn, B-9000 Ghent, Belgium
[2] Univ Arizona, Dept Biochem, Tucson, AZ 85721 USA
关键词
tyrosine ammonia lyase; photoactive yellow protein; p-hydroxycinnamic acid; phenylalanine ammonia lyase; Rhodobacter capsulatus;
D O I
10.1016/S0014-5793(02)02272-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. (C) 2002 Federation of European Biochemical Societies. Published by, Elsevier Science B.V. All rights reserved.
引用
收藏
页码:240 / 244
页数:5
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