Any feedback?
Literature summary extracted from
- Crystallographic symmetry and coenzyme binding properties of D-glyceraldehyde-3-phosphate dehydrogenase from the tail muscle of Palinurus vulgaris (1979), J. Biol. Chem., 254, 8004-8006.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.2.1.12 | - |
Palinurus vulgaris |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.2.1.12 | Palinurus vulgaris | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.2.1.12 | muscle | tail muscle | Palinurus vulgaris | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Palinurus vulgaris | 3-phospho-D-glyceroyl phosphate + NADH | - |
? |  |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.2.1.12 | NAD+ | the binding of NAD+ to apoenzyme in solution at 25°C is anticooperative | Palinurus vulgaris | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
