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Literature summary for 1.14.19.54 extracted from

  • Hirata, K.; Poeaknapo, C.; Schmidt, J.; Zenk, M.H.
    1,2-Dehydroreticuline synthase, the branch point enzyme opening the morphinan biosynthetic pathway (2004), Phytochemistry, 65, 1039-1046 .
    View publication on PubMed

Application

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 [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.117
-
(S)-reticuline pH 8.7, 35°C Papaver somniferum

Localization

Localization Comment Organism GeneOntology No. Textmining
vesicle enzyme occurs in particles of different densities Papaver somniferum 31982
-

Organism

Organism UniProt Comment Textmining
Papaver somniferum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
from seedling Papaver somniferum

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
Papaver somniferum
-

Storage Stability

Storage Stability Organism
enzyme is sensitive to freezing Papaver somniferum

Substrates and Products (Substrate)

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Papaver somniferum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
27
-
50% of maximum activity Papaver somniferum
55
-
50% of maximum activity Papaver somniferum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.8
-
-
Papaver somniferum

pH Range

pH Minimum pH Maximum Comment Organism
8
-
50% of maximum activity Papaver somniferum
9.5
-
50% of maximum activity Papaver somniferum

Cofactor

Cofactor Comment Organism Structure
additional information enzyme does not need a redox cofactor Papaver somniferum

General Information

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