The role of pyridoxal phosphate in the function of EspB, a protein secreted by enteropathogenic Escherichia coli

FEBS Letters

Donnenberg, Michael S.²  Taylor, Kathleen A.²  O'Connell, Colin B.¹  Thompson, Richard³ 

[1] Department of Microbiology and Immunology, University of Maryland School of Medicine, 10 South Pine Street, MSTF-900, Baltimore, MD 21201, USA;Division of Infectious Diseases, Department of Medicine, University of Maryland School of Medicine, 10 South Pine Street, MSTF-900, Baltimore, MD 21201, USA;Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 10 South Pine Street, MSTF-900, Baltimore, MD 21201, USA

关键词: Protein secretion;    Pyridoxal phosphate;    Bacterial pathogenesis;    Fluorometry;    Enteropathogenic Escherichia coli;   

DOI  :  10.1016/S0014-5793(00)02384-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown