Thymidine diphosphate-6-deoxy-L-lyxo-4-hexulose reductase synthesizing dTDP-6-deoxy-L-talose from Actinobacillus actinomycetemcomitans

Yoshio Nakano, Nao Suzuki, Yasuo Yoshida, Takashi Nezu, Yoshihisa Yamashita, Toshihiko Koga

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

The serotype c-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans NCTC 9710 contains an unusual sugar, 6-deoxy-L-talose, which has been identified as a constituent of cell wall components in some bacteria. Two genes coding for thymidine diphosphate (dTDP)-6-deoxy-L-lyxo-4- hexulose reductases were identified in the gene cluster required for biosynthesis of serotype c-specific polysaccharide. Both dTDP-6-deoxy-L-4- lyxo-4-hexulose reductases were overproduced and purified from Escherichia coli transformed with the plasmids containing these genes. The sugar nucleotides converted by both reductases were purified by reversed phase high performance liquid chromatography and identified by 1H nuclear magnetic resonance and gas-liquid chromatography. The results indicated that one of two reductases produced dTDP-6-deoxy-L-talose and the other produced dTDP-L- rhamnose (dTDP-6-deoxy-L-mannose). The amino acid sequence of the dTDP-6- deoxy-L-lyxo-4-hexulose reductase forming dTDP-6-deoxy-L-talose shared only weak homology with that forming dTDP-L-rhamnose, despite the fact that these two enzymes catalyze the reduction of the same substrate and the products are determined by the stereospecificity of the reductase activity. Neither the gene for dTDP-6-deoxy-L-talose biosynthesis nor its corresponding protein product has been found in other bacteria; this biosynthetic pathway is identified here for the first time.

Original languageEnglish
Pages (from-to)6806-6812
Number of pages7
JournalJournal of Biological Chemistry
Volume275
Issue number10
DOIs
Publication statusPublished - Mar 10 2000

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Aggregatibacter actinomycetemcomitans
Oxidoreductases
Genes
Biosynthesis
Sugars
Polysaccharides
Bacteria
Rhamnose
Diphosphates
Biosynthetic Pathways
Liquid chromatography
High performance liquid chromatography
Reverse-Phase Chromatography
Cellular Structures
Mannose
Multigene Family
Gas chromatography
Gas Chromatography
Thymidine
Cell Wall

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Thymidine diphosphate-6-deoxy-L-lyxo-4-hexulose reductase synthesizing dTDP-6-deoxy-L-talose from Actinobacillus actinomycetemcomitans. / Nakano, Yoshio; Suzuki, Nao; Yoshida, Yasuo; Nezu, Takashi; Yamashita, Yoshihisa; Koga, Toshihiko.

In: Journal of Biological Chemistry, Vol. 275, No. 10, 10.03.2000, p. 6806-6812.

Research output: Contribution to journalArticle

Nakano, Yoshio ; Suzuki, Nao ; Yoshida, Yasuo ; Nezu, Takashi ; Yamashita, Yoshihisa ; Koga, Toshihiko. / Thymidine diphosphate-6-deoxy-L-lyxo-4-hexulose reductase synthesizing dTDP-6-deoxy-L-talose from Actinobacillus actinomycetemcomitans. In: Journal of Biological Chemistry. 2000 ; Vol. 275, No. 10. pp. 6806-6812.
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abstract = "The serotype c-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans NCTC 9710 contains an unusual sugar, 6-deoxy-L-talose, which has been identified as a constituent of cell wall components in some bacteria. Two genes coding for thymidine diphosphate (dTDP)-6-deoxy-L-lyxo-4- hexulose reductases were identified in the gene cluster required for biosynthesis of serotype c-specific polysaccharide. Both dTDP-6-deoxy-L-4- lyxo-4-hexulose reductases were overproduced and purified from Escherichia coli transformed with the plasmids containing these genes. The sugar nucleotides converted by both reductases were purified by reversed phase high performance liquid chromatography and identified by 1H nuclear magnetic resonance and gas-liquid chromatography. The results indicated that one of two reductases produced dTDP-6-deoxy-L-talose and the other produced dTDP-L- rhamnose (dTDP-6-deoxy-L-mannose). The amino acid sequence of the dTDP-6- deoxy-L-lyxo-4-hexulose reductase forming dTDP-6-deoxy-L-talose shared only weak homology with that forming dTDP-L-rhamnose, despite the fact that these two enzymes catalyze the reduction of the same substrate and the products are determined by the stereospecificity of the reductase activity. Neither the gene for dTDP-6-deoxy-L-talose biosynthesis nor its corresponding protein product has been found in other bacteria; this biosynthetic pathway is identified here for the first time.",
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