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Papers In Press, published online ahead of print July 30, 2001
Biology, Johns Hopkins University, Baltimore, Maryland 21218
Corresponding Author: zoot{at}jhu.edu
Summary 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. Micro.36, 174-182], the primary Gram-negative bacterium causing meningitis in newborns, has been cloned and expressed in Escherichia 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- phosphate with a preference for diadenosine pentaphosphate, from which it forms ATP and ADP. The enzyme has an optimum 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.
J. Biol. Chem, 10.1074/jbc.M107032200
Submitted on July 24, 2001
Revised on July 30, 2001
Accepted on July 28, 2001
The gene, ygdP, associated with the invasiveness of Escherichia coli K1, designates a nudix hydrolase (Orf 176) active on Adenosine (5') pentaphospho (5') adenosine
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