PMID:11479323
| Citation |
Bessman, MJ, Walsh, JD, Dunn, CA, Swaminathan, J, Weldon, JE and Shen, J (2001) The gene ygdP, associated with the invasiveness of Escherichia coli K1, designates a Nudix hydrolase, Orf176, active on adenosine (5')-pentaphospho-(5')-adenosine (Ap5A). J. Biol. Chem. 276:37834-8 |
|---|---|
| Abstract |
ygdP, a gene associated with the invasion of brain microvascular endothelial cells by Escherichia coli K1 (Badger, J. L., Wass, C. A., and Kim, K. S. (2000) Mol. Microbiol. 36, 174-182), the primary Gram-negative bacterium causing meningitis in newborns, has been cloned and expressed in E. coli. The protein, YgdP, was purified to near homogeneity and identified as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate pyrophosphatases. It catalyzes the hydrolysis of diadenosine tetra-, penta-, and hexa-phosphates with a preference for diadenosine penta-phosphate, from which it forms ATP and ADP. The enzyme has a requirement for a divalent metal cation that can be met with Mg2+, Zn2+, or Mn2+ and, like most of the Nudix hydrolases, has an alkaline pH optimum between 8.5 and 9. This is the second identification of a gene associated with the invasiveness of a human pathogen as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate pyrophosphatases, and an examination of homologous proteins in other invasive bacteria suggests that this may be a common feature of cellular invasion. |
| Links |
PubMed Online version:10.1074/jbc.M107032200 |
| Keywords |
Amino Acid Sequence; Dinucleoside Phosphates/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/genetics; Escherichia coli/pathogenicity; Genes, Bacterial; Molecular Sequence Data; Open Reading Frames; Pyrophosphatases/chemistry; Pyrophosphatases/genetics; Pyrophosphatases/isolation & purification; Pyrophosphatases/physiology; Sequence Homology, Amino Acid; Substrate Specificity; Virulence/genetics |
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