EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.2.1.9 | 3-phospho-D-glycerate + NADH + H+ |
- |
Synechococcus sp. |
D-glyceraldehyde 3-phosphate + NAD+ + H2O |
- |
r |
1.2.1.9 | 3-phospho-D-glyceroyl phosphate + NADPH + H+ |
- |
Chlamydomonas reinhardtii |
D-glyceraldehyde 3-phosphate + phosphate + NADP+ |
- |
? |
1.2.1.9 | 3-phospho-D-glyceroyl phosphate + NADPH + H+ |
- |
Spinacia oleracea |
D-glyceraldehyde 3-phosphate + phosphate + NADP+ |
- |
? |
1.2.1.9 | D-glyceraldehyde 3-phosphate + H2O + NADP+ |
- |
Arabidopsis thaliana |
(2R)-3-phosphoglycerate + NADPH + 2 H+ |
- |
? |
1.2.1.9 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
- |
Hevea brasiliensis |
3-phospho-D-glycerate + NADH + H+ |
- |
r |
1.2.1.9 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
enzyme shows negligible activity with NAD+. The NAD+-dependent reaction shows no saturation at NAD+ concentrations up to 50 mM. The highest enzyme activity is observed at 50 mM NAD+ which is 7fold to 8fold lower than the Vmax observed using NADP+ as cofactor |
Saccharolobus solfataricus |
3-phospho-D-glycerate + NADH + H+ |
- |
ir |
1.2.1.9 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
NAD+ is a poor co-substrate |
Sulfurisphaera tokodaii |
3-phospho-D-glycerate + NADH + H+ |
- |
? |
1.2.1.9 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM |
Sulfurisphaera tokodaii |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
1.2.1.9 | D-glyceraldehyde 3-phosphate + NAD+ + H2O |
the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM |
Sulfurisphaera tokodaii 7 |
3-phospho-D-glycerate + NADH + 2 H+ |
- |
ir |
1.2.1.9 | D-glyceraldehyde 3-phosphate + NADP+ + H2O |
- |
Chlamydomonas reinhardtii |
3-phospho-D-glycerate + NADPH + H+ |
- |
? |