Literature summary extracted from
Kudo, F.; Yamauchi, N.; Suzuki, R.; Kakinuma, K.
Kinetic isotope effect and reaction mechanism of 2-deoxy-scyllo-inosose synthase derived from butirosin-producing Bacillus circulans (1997), J. Antibiot., 50, 424-428.
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.2.3.124 |
Co2+ |
required |
Niallia circulans |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.2.3.124 |
D-glucose 6-phosphate |
Niallia circulans |
intramolecular carbocyclization, mechanism, overview |
2-deoxy-L-scyllo-inosose + phosphate |
- |
? |
|
4.2.3.124 |
D-glucose 6-phosphate |
Niallia circulans SANK72073 |
intramolecular carbocyclization, mechanism, overview |
2-deoxy-L-scyllo-inosose + phosphate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.3.124 |
Niallia circulans |
Q9S5E2 |
gene btrC, a butirosin producing strain |
- |
4.2.3.124 |
Niallia circulans SANK72073 |
Q9S5E2 |
gene btrC, a butirosin producing strain |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.2.3.124 |
native enzyme by ammonium sulfate fractionation, dialysis and two different steps of anion exchange chromatography |
Niallia circulans |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
4.2.3.124 |
D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate |
reaction mechanism, overview |
Niallia circulans |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.3.124 |
D-glucose 6-phosphate |
intramolecular carbocyclization, mechanism, overview |
Niallia circulans |
2-deoxy-L-scyllo-inosose + phosphate |
- |
? |
|
4.2.3.124 |
D-glucose 6-phosphate |
intramolecular carbocyclization, hydride abstraction and returning appeared to take place within the same glucose molecule |
Niallia circulans |
2-deoxy-L-scyllo-inosose + phosphate |
product identification by GC-MS analysis |
? |
|
4.2.3.124 |
D-glucose 6-phosphate |
intramolecular carbocyclization, mechanism, overview |
Niallia circulans SANK72073 |
2-deoxy-L-scyllo-inosose + phosphate |
- |
? |
|
4.2.3.124 |
D-glucose 6-phosphate |
intramolecular carbocyclization, hydride abstraction and returning appeared to take place within the same glucose molecule |
Niallia circulans SANK72073 |
2-deoxy-L-scyllo-inosose + phosphate |
product identification by GC-MS analysis |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.3.124 |
DOI synthase |
- |
Niallia circulans |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
4.2.3.124 |
37 |
- |
assay at |
Niallia circulans |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
4.2.3.124 |
7.5 |
- |
assay at |
Niallia circulans |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.2.3.124 |
NAD+ |
essential for activity |
Niallia circulans |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
4.2.3.124 |
physiological function |
the enzyme is crucial in the carbocyclization reaction as part of the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics. The DOI synthase catalyzes the intramolecular carbocyclization of D-glucose 6-phosphate into the first non-aminogenous cyclitol 2-deoxy-L-scyllo-inosose, DOI |
Niallia circulans |