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Literature summary for 1.1.1.361 extracted from

  • Vetter, N.D.; Langill, D.M.; Anjum, S.; Boisvert-Martel, J.; Jagdhane, R.C.; Omene, E.; Zheng, H.; van Straaten, K.E.; Asiamah, I.; Krol, E.S.; Sanders, D.A.; Palmer, D.R.
    A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis (2013), J. Am. Chem. Soc., 135, 5970-5973.
    View publication on PubMed
Search for more literature for 1.1.1.361

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + NAD+ poor substrate Bacillus subtilis 3-dehydro-D-glucose + NADH + H+
-
 ?
D-glucose 6-phosphate + NAD+
-
 Bacillus subtilis 3-dehydro-D-glucose 6-phosphate + NADH + H+
-
 ?
inositol + NAD+ poor substrate Bacillus subtilis ? + NADH + H+
-
 ?
additional information no substrate: UDP-glucose Bacillus subtilis ?
-
 ?

Synonyms

Synonyms Comment Organism
ntdC
-
 Bacillus subtilis
yhjJ
-
 Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
additional information no cofactor: NADP+ Bacillus subtilis
NAD+ highly specific Bacillus subtilis

General Information

General Information Comment Organism
physiological function the ntd operon is essential for biosynthesis of the unusual disaccharide 3,3'-neotrehalosadiamine. The enzymes catalyze the biosynthesis of kanosamine from D-glucose 6-phosphate. NtdC is a D-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 Bacillus subtilis