EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.370 | L-epi-2-inosose + NADH + H+ |
- |
Paracoccus laeviglucosivorans |
myo-inositol + NAD+ |
- |
r |
1.1.1.370 | more |
the enzyme performs also reversible L-glucose oxidation, structural basis and kinetics, overview. Substrate binding structures, detailed overview. Pl-scyllo-IDH has a different regioselectivity compared to myo-IDH toward myo-inositol |
Paracoccus laeviglucosivorans |
? |
- |
- |
1.1.1.370 | myo-inositol + NAD+ |
- |
Paracoccus laeviglucosivorans |
L-epi-2-inosose + NADH + H+ |
- |
r |
1.1.1.370 | scyllo-inositol + NAD+ |
- |
Bacillus subtilis |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
- |
? |
1.1.1.370 | scyllo-inositol + NAD+ |
- |
Paracoccus laeviglucosivorans |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
- |
r |
1.1.1.370 | scyllo-inositol + NAD+ |
no activity with NADP+ |
Bacillus subtilis |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
2,4,6/3,5-pentahydroxycyclohexanone i.e. (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone i.e. scyllo-inosose |
r |
1.1.1.370 | scyllo-inositol + NAD+ |
the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA |
Bacillus subtilis |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
- |
r |
1.1.1.370 | scyllo-inositol + NAD+ |
no activity with NADP+ |
Bacillus subtilis 168 |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
2,4,6/3,5-pentahydroxycyclohexanone i.e. (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone i.e. scyllo-inosose |
r |
1.1.1.370 | scyllo-inositol + NAD+ |
the enzyme is part of a scyllo-inositol degradation pathway leading to acetyl-CoA |
Bacillus subtilis 168 |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
- |
r |
1.1.1.370 | scyllo-inositol + NAD+ |
- |
Bacillus subtilis 168 |
2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+ |
- |
? |