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Journal of Bacteriology, June 2006, p. 4153-4157, Vol. 188, No. 11
0021-9193/06/$08.00+0 doi:10.1128/JB.01926-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Department of Biological Chemistry, Institute of Molecular Biology and Physiology, University of Copenhagen, Sølvgade 83 H, 1307 Copenhagen K, Denmark
Received 16 December 2005/ Accepted 20 March 2006
xapABR from Salmonella enterica was analyzed and compared with the corresponding Escherichia coli genes. xapB and xapR, but not xapA, encode functional proteins. An S. enterica XapA(Asp72Gly) mutant that restores the phosphorolytic activity was selected. The purified mutant enzyme has different kinetic constants than the E. coli enzyme but similar substrate specificity.
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