EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
4.2.1.164 | dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ |
the enzyme participates in the biosynthesis of forosamine, a key structural component of the spinosyns, which are produced by Saccharopolyspora spinosa |
Saccharopolyspora spinosa |
dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster |
- |
? |
4.2.1.164 | dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ |
the enzyme requires ferredoxin/ferredoxin reductase or flavodoxin/flavodoxin reductase. It can act as a transaminase when the electron-transfer path is blocked |
Saccharopolyspora spinosa |
dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster |
- |
? |
4.2.1.164 | dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ |
the enzyme is involved in TDP-D-forosamine biosynthesis in the spinosyn pathway |
Saccharopolyspora spinosa |
dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster |
- |
? |
4.2.1.164 | dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ |
the enzyme is capable of catalyzing C-3 deoxygenation in the presence of dithionite or the reductase pairs ferredoxin/ferredoxin reductase or flavodoxin/flavodoxin reductase. Conversion is significantly more efficient using reductase pairs than using dithionite. In the absence of an electron source and in the presence of L-glutamate, SpnQ catalyzes a transamination reaction, converting dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose to TDP-4-amino-2,4,6-trideoxy-D-glucose |
Saccharopolyspora spinosa |
dTDP-4-dehydro-2,3,6-trideoxy-alpha-D-hexopyranose + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster |
- |
? |
4.2.1.164 | more |
TDP-4-dehydro-6-deoxy-D-glucose is not a substrate |
Saccharopolyspora spinosa |
? |
- |
? |