Crystallization (Comment) | Organism |
---|---|
X-ray diffraction structure determination and analysis at 2.4 A resolution, structure modeling | Acropora millepora |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Acropora millepora | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acropora millepora | A0A3F2YLZ0 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Acropora millepora | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | - |
Acropora millepora |
Synonyms | Comment | Organism |
---|---|---|
glyceraldehyde-3-phosphate dehydrogenase | - |
Acropora millepora |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the thermal stability of glyceraldehyde-3-phosphate dehydrogenase increases significantly in the presence of its cofactor NAD+. Incubation of Acropora millepora GAPDH with NAD+ increases its melting temperature by 15°C | Acropora millepora |
63.2 | - |
enzyme without NAD+ | Acropora millepora |
78.4 | - |
NAD+-bound enzyme | Acropora millepora |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | analysis of the structure of the cofactor-enzyme complex (PDB ID 6PX2) reveals variable NAD+ occupancy across the four monomers of the tetrameric enzyme. The NAD+ binding sites of the tetramer are occupied to different extents, overview | Acropora millepora |
General Information | Comment | Organism |
---|---|---|
metabolism | glyceraldehyde-3-phosphate dehydrogenase is a critical metabolic enzyme in the stony coral Acropora millepora | Acropora millepora |
additional information | the GAPDH enzyme from the reef-building stony coral Acropora millepora is a rather typical eukaryotic GAPDH, comprising an N-terminal NAD+-binding Rossman fold and a catalytic domain that provides important active site residues | Acropora millepora |