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Literature summary for 1.14.14.36 extracted from
- Isolation of the heme-thiolate enzyme chytochrome P-450tyr, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench (1994), Proc. Natl. Acad. Sci. USA, 91, 9740-9744.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Sorghum bicolor | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 57000 | - |
SDS-PAGE | Sorghum bicolor |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sorghum bicolor | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| combined use of Renex 690, CHAPS and RTX-100 is optimal for maximal recovery and avoidance of conversion into cytochrome P-420 | Sorghum bicolor |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] | high substrate specificity | Sorghum bicolor | N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? |  |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9.5 | - |
Sorghum bicolor |
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Release 2023.1 (January 2023)
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