Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.361 expression in Escherichia coli Bacillus subtilis
2.6.1.104 expression of the N-terminal hexahistidine-tagged protein in Escherichia coli Bacillus subtilis
3.1.3.92 expression in 'Escherichia coli Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.92 0.101
-
kanosamine 6-phosphate pH not specified in the publication, temperature not specified in the publication Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.104 kanosamine 6-phosphate + 2-oxoglutarate Bacillus subtilis the enzyme is involved in a kanosamine biosynthesis pathway 3-dehydro-D-glucose 6-phosphate + L-glutamate
-
?
2.6.1.104 kanosamine 6-phosphate + 2-oxoglutarate Bacillus subtilis 168 the enzyme is involved in a kanosamine biosynthesis pathway 3-dehydro-D-glucose 6-phosphate + L-glutamate
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.361 Bacillus subtilis
-
-
-
2.6.1.104 Bacillus subtilis O07566
-
-
2.6.1.104 Bacillus subtilis 168 O07566
-
-
3.1.3.92 Bacillus subtilis O07565
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.361 D-glucose + NAD+ poor substrate Bacillus subtilis 3-dehydro-D-glucose + NADH + H+
-
?
1.1.1.361 D-glucose 6-phosphate + NAD+
-
Bacillus subtilis 3-dehydro-D-glucose 6-phosphate + NADH + H+
-
?
1.1.1.361 inositol + NAD+ poor substrate Bacillus subtilis ? + NADH + H+
-
?
1.1.1.361 additional information no substrate: UDP-glucose Bacillus subtilis ?
-
?
2.6.1.104 kanosamine 6-phosphate + 2-oxoglutarate
-
Bacillus subtilis 3-dehydro-D-glucose 6-phosphate + L-glutamate
-
?
2.6.1.104 kanosamine 6-phosphate + 2-oxoglutarate the enzyme is involved in a kanosamine biosynthesis pathway Bacillus subtilis 3-dehydro-D-glucose 6-phosphate + L-glutamate
-
?
2.6.1.104 kanosamine 6-phosphate + 2-oxoglutarate
-
Bacillus subtilis 168 3-dehydro-D-glucose 6-phosphate + L-glutamate
-
?
2.6.1.104 kanosamine 6-phosphate + 2-oxoglutarate the enzyme is involved in a kanosamine biosynthesis pathway Bacillus subtilis 168 3-dehydro-D-glucose 6-phosphate + L-glutamate
-
?
3.1.3.92 D-glucosamine 6-phosphate + H2O about 1% of the activity with kanosamine 6-phosphate Bacillus subtilis D-glucosamine + phosphate
-
?
3.1.3.92 kanosamine 6-phosphate + H2O
-
Bacillus subtilis kanosamine + phosphate
-
?
3.1.3.92 additional information no substrates: glucose 6-phosphate, 4-nitrophenyl phosphate, 3,3'-neotrehalosediamine 6-phosphate, 3,3'-neotrehalosediamine 6'-phosphate, 3,3'-neotrehalosediamine 6,6'-bisphosphate, glucose 1-phosphate Bacillus subtilis ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.361 ntdC
-
Bacillus subtilis
1.1.1.361 yhjJ
-
Bacillus subtilis
2.6.1.104 3-oxo-glucose-6-phosphate:glutamate aminotransferase
-
Bacillus subtilis
2.6.1.104 ntdA
-
Bacillus subtilis
3.1.3.92 ntdB
-
Bacillus subtilis
3.1.3.92 yhjK
-
Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.92 32
-
kanosamine 6-phosphate pH not specified in the publication, temperature not specified in the publication Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.361 additional information no cofactor: NADP+ Bacillus subtilis
1.1.1.361 NAD+ highly specific Bacillus subtilis
2.6.1.104 pyridoxal 5'-phosphate a pyridoxal-phosphate protein Bacillus subtilis

General Information

EC Number General Information Comment Organism
1.1.1.361 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
2.6.1.104 physiological function the enzyme is involved in a kanosamine biosynthesis pathway Bacillus subtilis
3.1.3.92 physiological function the ntd operon is essential for biosynthesis of the unusual disaccharide 3,3'-neotrehalosadiamine. The 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 Bacillus subtilis