Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosynthesis

被引:79
作者
Kupke, T
Uebele, M
Schmid, D
Jung, G
Blaesse, M
Steinbacher, S
机构
[1] Univ Tubingen, Lehrstuhl Mikrobielle Genet, D-72076 Tubingen, Germany
[2] Univ Tubingen, Inst Organ Chem, D-72076 Tubingen, Germany
[3] Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Planegg Martinsried, Germany
关键词
D O I
10.1074/jbc.M004273200
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
The lantibiotic-synthesizing flavoprotein EpiD catalyzes the oxidative decarboxylation of peptidylcysteines to peptidyl-aminoenethiols. The sequence motif responsible for flavin coenzyme binding and enzyme activity is conserved in different proteins from all kingdoms of life. Dfp proteins of eubacteria and archaebacteria and salt tolerance proteins of yeasts and plants belong to this new family of flavoproteins. The enzymatic function of all these proteins was not known, but our experiments suggested that they catalyze a similar reaction like EpiD and/or may have similar substrates and are homododecameric flavoproteins. We demonstrate that the N-terminal domain of the Escherichia coli Dfp protein catalyzes the decarboxylation of (R)-4'-phospho-N-pantothenoylcysteine to 4'-phosphopantetheine. This reaction is essential for coenzyme A biosynthesis.
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收藏
页码:31838 / 31846
页数:9
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