A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis

J Am Chem Soc. 2013 Apr 24;135(16):5970-3. doi: 10.1021/ja4010255. Epub 2013 Apr 15.


The ntd operon in Bacillus subtilis is essential for biosynthesis of 3,3'-neotrehalosadiamine (NTD), an unusual nonreducing disaccharide reported to have antibiotic properties. It has been proposed that the three enzymes encoded within this operon, NtdA, NtdB, and NtdC, constitute a complete set of enzymes required for NTD synthesis, although their functions have never been demonstrated in vitro. We now report that these enzymes catalyze the biosynthesis of kanosamine from glucose-6-phosphate: NtdC is a glucose-6-phosphate 3-dehydrogenase, NtdA is a pyridoxal phosphate-dependent 3-oxo-glucose-6-phosphate:glutamate aminotransferase, and NtdB is a kanosamine-6-phosphate phosphatase. None of these enzymatic reactions have been reported before. This pathway represents an alternate route to the previously reported pathway from Amycolatopsis mediterranei which derives kanosamine from UDP-glucose.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / biosynthesis*
  • Bacillus subtilis / genetics
  • Bacillus subtilis / metabolism*
  • Glucosamine / biosynthesis
  • Glucose-6-Phosphate / metabolism
  • Operon / genetics
  • Pyridoxal Phosphate / metabolism
  • Spectrophotometry, Ultraviolet
  • Trehalose / analogs & derivatives
  • Uridine Diphosphate Glucose / metabolism


  • Anti-Bacterial Agents
  • 3,3'-neotrehalosadiamine
  • Glucose-6-Phosphate
  • kanosamine
  • Pyridoxal Phosphate
  • Trehalose
  • Glucosamine
  • Uridine Diphosphate Glucose