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Literature summary for 1.2.1.12 extracted from
- Effect of association-dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenase (1979), Arch. Biochem. Biophys., 193, 28-33.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | activity depends non-linearly on protein concentration in the range 0.00003-0.003 mM. With increasing concentrations the apparently hyperbolic substrate saturation curves turn into sigmoidal ones | Oryctolagus cuniculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| muscle | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Oryctolagus cuniculus | 3-phospho-D-glyceroyl phosphate + NADH | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme exists as an equilibrium mixture of different oligomeric states. Rapid equilibrium between monomer - dimer - tetramer, the tetramer is inactive | Oryctolagus cuniculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Oryctolagus cuniculus | |
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Release 2023.1 (January 2023)
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