BRENDA - Enzyme Database
show all sequences of 1.14.19.54

1,2-Dehydroreticuline synthase, the branch point enzyme opening the morphinan biosynthetic pathway

Hirata, K.; Poeaknapo, C.; Schmidt, J.; Zenk, M.H.; Phytochemistry 65, 1039-1046 (2004)

Data extracted from this reference:

Application
Application
Commentary
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
Commentary
Organism
Structure
0.117
-
(S)-reticuline
pH 8.7, 35°C
Papaver somniferum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
vesicle
enzyme occurs in particles of different densities
Papaver somniferum
31982
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Papaver somniferum
-
-
-
Purification (Commentary)
Commentary
Organism
from seedling
Papaver somniferum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
seedling
-
Papaver somniferum
-
Storage Stability
Storage Stability
Organism
enzyme is sensitive to freezing
Papaver somniferum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-norreticuline + [reduced NADPH-hemoprotein reductase] + O2
-
746006
Papaver somniferum
1,2-dehydronorreticuline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(S)-reticuline + [reduced NADPH-hemoprotein reductase] + O2
-
746006
Papaver somniferum
1,2-dehydroreticuline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
additional information
enzyme accepts both (S)-reticuline and (S)-norreticuline as substrates
746006
Papaver somniferum
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Papaver somniferum
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
27
-
50% of maximum activity
Papaver somniferum
55
-
50% of maximum activity
Papaver somniferum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
-
Papaver somniferum
pH Range
pH Minimum
pH Maximum
Commentary
Organism
8
-
50% of maximum activity
Papaver somniferum
9.5
-
50% of maximum activity
Papaver somniferum
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
enzyme does not need a redox cofactor
Papaver somniferum
Application (protein specific)
Application
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
enzyme does not need a redox cofactor
Papaver somniferum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.117
-
(S)-reticuline
pH 8.7, 35°C
Papaver somniferum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
vesicle
enzyme occurs in particles of different densities
Papaver somniferum
31982
-
Purification (Commentary) (protein specific)
Commentary
Organism
from seedling
Papaver somniferum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
seedling
-
Papaver somniferum
-
Storage Stability (protein specific)
Storage Stability
Organism
enzyme is sensitive to freezing
Papaver somniferum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-norreticuline + [reduced NADPH-hemoprotein reductase] + O2
-
746006
Papaver somniferum
1,2-dehydronorreticuline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(S)-reticuline + [reduced NADPH-hemoprotein reductase] + O2
-
746006
Papaver somniferum
1,2-dehydroreticuline + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
additional information
enzyme accepts both (S)-reticuline and (S)-norreticuline as substrates
746006
Papaver somniferum
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Papaver somniferum
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
27
-
50% of maximum activity
Papaver somniferum
55
-
50% of maximum activity
Papaver somniferum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
-
Papaver somniferum
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
8
-
50% of maximum activity
Papaver somniferum
9.5
-
50% of maximum activity
Papaver somniferum
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 1.14.19.54
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743332
Farrow
Stereochemical inversion of ( ...
Papaver rhoeas, Papaver somniferum
Nat. Chem. Biol.
11
728-732
2015
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
743843
Winzer
Plant science. Morphinan bios ...
Papaver somniferum
Science
349
309-312
2015
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
746006
Hirata
1,2-Dehydroreticuline synthas ...
Papaver somniferum
Phytochemistry
65
1039-1046
2004
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
-
1
-
-
1
-
1
3
-
1
2
-
-
1
2
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
1
-
1
3
-
1
2
-
-
1
2
-
-
-
1
1
-
-
-