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Literature summary extracted from
- Spectroscopic and kinetic characterization of the bifunctional chorismate synthase from Neurospora crassa: evidence for a common binding site for 5-enolpyruvylshikimate 3-phosphate and NADPH (2001), J. Biol. Chem., 276, 42658-42666.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.3.5 | expression in Escherichia coli | Neurospora crassa |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.3.5 | Neurospora crassa | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.3.5 | - |
Neurospora crassa |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.3.5 | FMN + NADPH | recombinant enzyme has a diaphorase activity. NADPH binds in or near the substrate (O5-(1-carboxyvinyl)-3-phosphoshikimate) binding site, suggesting that NADPH binding to the enzyme is embedded in the general protein structure and a special NADPH binding domain is not required to generate the intrinsic oxidoreductase activity | Neurospora crassa | ? | - |
? |  |
| 4.2.3.5 | O5-(1-carboxyvinyl)-3-phosphoshikimate | - |
Neurospora crassa | chorismate + phosphate | - |
? | |
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Release 2023.1 (January 2023)
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