ArticleJournal of bacteriology2000
Genetic and biochemical characterization of Salmonella enterica serovar typhi deoxyribokinase.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Protein STM3547 From Salmonella typhimurium Is a Phosphofructose Kinase B-Type Enzyme With Ribose Kinase Activity.Molecular microbiology · 2026Article
- Dependence ofApplied and environmental microbiology · 2026Article
- Enzyme promiscuity shapes adaptation to novel growth substrates.Molecular systems biology · 2019Article
- Ribose utilization by the human commensal Bifidobacterium breve UCC2003.Microbial biotechnology · 2010Article
- Role of deoxyribose catabolism in colonization of the murine intestine by pathogenic Escherichia coli strains.Infection and immunity · 2009Article
- Use of deoxyribose by intestinal and extraintestinal pathogenic Escherichia coli strains: a metabolic adaptation involved in competitiveness.Infection and immunity · 2004Article
- Deciphering the function of an ORF: Salmonella enterica DeoM protein is a new mutarotase specific for deoxyribose.Protein science : a publication of the Protein Society · 2004Article
- Regulation of expression of the 2-deoxy-D-ribose utilization regulon, deoQKPX, from Salmonella enterica serovar typhimurium.Journal of bacteriology · 2003Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 V(max) of deoxyribokinase by a factor of 2.5 and increased the K(m) for deoxyribose by a factor of 70, compared to the parent enzyme.
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