Application | Comment | Organism |
---|---|---|
analysis | [1-2H, 13C]-(R,S)-reticuline is enzymatically converted into [1-13C]-dehydroreticuline. Release of the hydrogen atom in position C-1 of the isoquinoline alkaloid during the oxidative conversion can be exploited as a sensitive assay system for the enzyme | Papaver somniferum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.117 | - |
(S)-reticuline | pH 8.7, 35°C | Papaver somniferum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
vesicle | enzyme occurs in particles of different densities | Papaver somniferum | 31982 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Papaver somniferum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
from seedling | Papaver somniferum |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
seedling | - |
Papaver somniferum | - |
Storage Stability | Organism |
---|---|
enzyme is sensitive to freezing | Papaver somniferum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-norreticuline + [reduced NADPH-hemoprotein reductase] + O2 | - |
Papaver somniferum | 1,2-dehydronorreticuline + [oxidized NADPH-hemoprotein reductase] + 2 H2O | - |
? | |
(S)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 | - |
Papaver somniferum | 1,2-dehydroreticuline + [oxidized NADPH-hemoprotein reductase] + 2 H2O | - |
? | |
additional information | enzyme accepts both (S)-reticuline and (S)-norreticuline as substrates | Papaver somniferum | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Papaver somniferum |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
27 | - |
50% of maximum activity | Papaver somniferum |
55 | - |
50% of maximum activity | Papaver somniferum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.8 | - |
- |
Papaver somniferum |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8 | - |
50% of maximum activity | Papaver somniferum |
9.5 | - |
50% of maximum activity | Papaver somniferum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | enzyme does not need a redox cofactor | Papaver somniferum |
General Information | Comment | Organism |
---|---|---|
physiological function | enzyme provides the necessary inversion of configuration and completes the pathway from two molecules of L-tyrosine via (S)-norcoclaurine to (R)-reticuline in opium poppy involving a total number of 11 enzymes | Papaver somniferum |