EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.388 | D-glucose 6-phosphate + NAD+ |
the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor |
Haloferax volcanii |
6-phospho-D-glucono-1,5-lactone + NADH + H+ |
- |
? |
1.1.1.388 | D-glucose 6-phosphate + NAD+ |
the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor |
Haloferax volcanii DSM 3757 |
6-phospho-D-glucono-1,5-lactone + NADH + H+ |
- |
? |
1.1.1.388 | D-glucose 6-phosphate + NADP+ |
the enzyme is functionally involved in pentose phosphate formation in vivo |
Haloferax volcanii |
6-phospho-D-glucono-1,5-lactone + NADPH + H+ |
- |
? |
1.1.1.388 | D-glucose 6-phosphate + NADP+ |
the enzyme is functionally involved in pentose phosphate formation in vivo |
Haloferax volcanii DSM 3757 |
6-phospho-D-glucono-1,5-lactone + NADPH + H+ |
- |
? |