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The role of pyridoxal phosphate in the function of EspB, a protein secreted by enteropathogenic Escherichia coli
Author(s) -
Taylor Kathleen A.,
O'Connell Colin B.,
Thompson Richard,
Donnenberg Michael S.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02384-x
Subject(s) - pyridoxal , enteropathogenic escherichia coli , escherichia coli , biochemistry , mutant , chemistry , microbiology and biotechnology , virulence , lysine , enzyme , biology , amino acid , gene
The sequence of EspB, a secreted protein required for virulence of enteropathogenic Escherichia coli (EPEC), reveals a motif common to enzymes that bind pyridoxal phosphate. Pyridoxal phosphate was not found by fluorometry in concentrated supernatants of EPEC cultures that contain EspB. Plasmids containing cloned espB , in which the lysine residue conserved in the motif was substituted with either an arginine or methionine residue, remained capable of complementing an espB deletion mutant to restore EspB function. The results of these studies do not support a role for pyridoxal phosphate in EspB function.