EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.12 | 2,3-diphosphoglycerate | - |
Glycine max | |
1.2.1.12 | AMP | - |
Glycine max | |
1.2.1.12 | NADH | competitive with respect to NAD+ and phosphate | Glycine max |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.1.12 | additional information | - |
additional information | - |
Glycine max |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.12 | Glycine max | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+ | bi-uni-uni-uni-ping-pong mechanism in which NAD+ and phosphate interact sequentially with the enzyme, followed in turn by the release of 3-phospho-D-glyceroyl phosphate, the addition of D-glyceraldehyde-3-phosphate, and the release of NADH. At pH 7.2, NAD+ binds to the enzyme in a rapid-equilibrium fashion, whereas at pH 8.8 there is rapid-equilibrium addition of both NAD+ and phosphate to the enzyme | Glycine max |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.2.1.12 | nodule | - |
Glycine max | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Glycine max | 3-phospho-D-glyceroyl phosphate + NADH | - |
? |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
1.2.1.12 | 8 | - |
very labile, especially above pH 8.0 | Glycine max |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.12 | NAD+ | at pH 8.8 there is rapid-equilibrium addition of both NAD+ and phosphate to the enzyme | Glycine max |