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Journal of Bacteriology, February 2000, p. 869-873, Vol. 182, No. 4
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Genetic and Biochemical Characterization of Salmonella enterica Serovar Typhi Deoxyribokinase

Lise Tourneux,1 Nadia Bucurenci,1,dagger Cosmin Saveanu,1,Dagger Pierre Alexandre Kaminski,2 Madeleine Bouzon,2 Elisabeth Pistotnik,1 Abdelkader Namane,1 Philippe Marlière,2 Octavian Bârzu,1 Inès Li de la Sierra,3 Jan Neuhard,4 and Anne-Marie Gilles1,*

Laboratoire de Chimie Structurale des Macromolécules,1 Unité de Biochimie Cellulaire,2 and Unité de Biochimie Structurale,3 Institut Pasteur, 75724 Paris Cedex 15, France, and Center for Enzyme Research, Institute of Molecular Biology, University of Copenhagen, Copenhagen K, Denmark4

Received 30 July 1999/Accepted 19 November 1999

We identified in the genome of Salmonella enterica serovar Typhi the gene encoding deoxyribokinase, deoK. Two other genes, vicinal to deoK, were determined to encode the putative deoxyribose transporter (deoP) and a repressor protein (deoQ). This locus, located between the uhpA and ilvN genes, is absent in Escherichia coli. The deoK gene inserted on a plasmid provides a selectable marker in E. coli for growth on deoxyribose-containing medium. Deoxyribokinase is a 306-amino-acid protein which exhibits about 35% identity with ribokinase from serovar Typhi, S. enterica serovar Typhimurium, or E. coli. The catalytic properties of the recombinant deoxyribokinase overproduced in E. coli correspond to those previously described for the enzyme isolated from serovar Typhimurium. From a sequence comparison between serovar Typhi deoxyribokinase and E. coli ribokinase, whose crystal structure was recently solved, we deduced that a key residue differentiating ribose and deoxyribose is Met10, which in ribokinase is replaced by Asn14. Replacement by site-directed mutagenesis of Met10 with Asn decreased the Vmax of deoxyribokinase by a factor of 2.5 and increased the Km for deoxyribose by a factor of 70, compared to the parent enzyme.

* Corresponding author. Mailing address: Laboratoire de Chimie Structurale des Macromolécules, Institut Pasteur, 28, rue du Dr. Roux, 75724 Paris Cedex 15, France. Phone: 33 (1) 45 68 89 68. Fax: 33 (1) 40 61 39 63. E-mail: amgilles{at}pasteur.fr.

dagger Permanent address: Institutul Cantacuzino, 70100 Bucharest, Romania.

Dagger Permanent address: Department of Biochemistry, University of Medicine and Pharmacy, Cluj-Napoca, Romania.

Journal of Bacteriology, February 2000, p. 869-873, Vol. 182, No. 4
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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