A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis.
J Am Chem Soc
; 135(16): 5970-3, 2013 Apr 24.
Article
en En
| MEDLINE
| ID: mdl-23586652
ABSTRACT
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-phosphateglutamate 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.
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Banco de datos:
MEDLINE
Asunto principal:
Bacillus subtilis
/
Antibacterianos
Idioma:
En
Revista:
J Am Chem Soc
Año:
2013
Tipo del documento:
Article