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Literature summary extracted from
- Biochemical and structural characterization of recombinant hyoscyamine 6beta-hydroxylase from Datura metel L (2010), Plant Physiol. Biochem., 48, 966-970 .
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.20.13 | 0.05 | - |
2-oxoglutarate | pH 7.8, 30°C | Datura metel |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.20.13 | Datura metel | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.20.13 | (6S)-6beta-hydroxyhyoscyamine + 2-oxoglutarate + O2 | - |
Datura metel | scopolamine + succinate + CO2 + H2O | - |
? | |
| 1.14.20.13 | additional information | enzyme catalyzes both the hydroxylation of hyoscyamine, reaction of EC 1.14.11.11, and the epoxidation of 6beta-hydroxyhyoscyamine to generate scopolamine. Epoxidase activity is low compared to the hydroxylase activity. The binding of the substrates, hyoscyamine and 2-oxoglutarate, to the enzyme induces significant conformational changes | Datura metel | ? | - |
? | |
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