Information on EC 1.5.1.27 - 1,2-dehydroreticulinium reductase (NADPH)

for references in articles please use BRENDA:EC1.5.1.27
Word Map on EC 1.5.1.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Papaver

EC NUMBER
COMMENTARY hide
1.5.1.27
-
RECOMMENDED NAME
GeneOntology No.
1,2-dehydroreticulinium reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-reticuline + NADP+ = 1,2-dehydroreticulinium + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
morphine biosynthesis
-
-
Isoquinoline alkaloid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
(R)-reticuline:NADP+ oxidoreductase
Reduces the 1,2-dehydroreticulinium ion to (R)-reticuline, which is a direct precursor of morphinan alkaloids in the poppy plant. The enzyme does not catalyse the reverse reaction to any significant extent under physiological conditions.
CAS REGISTRY NUMBER
COMMENTARY hide
130590-58-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Argemone hunnemannii
-
-
-
Manually annotated by BRENDA team
no activity in Dicentra spectabilis
-
-
-
Manually annotated by BRENDA team
no activity in Fumaria macrosepta
-
-
-
Manually annotated by BRENDA team
no activity in Papaver oreophilum
-
-
-
Manually annotated by BRENDA team
no activity in Papaver persicum
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the aldo-keto reductase family
physiological function
-
direction of metabolites to morphinan biosynthesis requires isomerization of (S)- to (R)-reticuline. The P450 module of the bifunctional enzyme is responsible for the conversion of (S)-reticuline to 1,2-dehydroreticuline, whereas the oxidoreductase module converts 1,2-dehydroreticuline to (R)-reticuline rather than functioning as a P450 redox partner. Proteomic analysis confirms that these two modules are contained on a single polypeptide in vivo
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-dehydro-N-methylcoclaurine NADPH + H+
N-methylcoclaurine + NADP+
show the reaction diagram
1,2-Dehydroreticuline + NADPH
(R)-Reticuline + NADP+
show the reaction diagram
1,2-Dehydroreticuline + NADPH
?
show the reaction diagram
1,2-dehydroreticulinium + NADPH + H+
(R)-reticuline + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,2-Dehydroreticuline + NADPH
?
show the reaction diagram
1,2-dehydroreticulinium + NADPH + H+
(R)-reticuline + NADP+
show the reaction diagram
additional information
?
-
P0DKI7
the bifunctional CYP82Y2 fusion enzyme termed reticuline epimerase (PsREPI) is a fusion between a cytochrome P450 (CYP) and an aldo-keto reductase (AKR) catalyzes the S-to-R epimerization of reticuline via 1,2-dehydroreticuline
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-reticuline
-
-
(S)-Coclaurine
-
-
(S)-N-methylcoclaurine
-
-
(S)-norreticuline
-
-
(S)-reticuline
-
-
6-O-methyllaudanosoline
-
-
salutaridine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
1,2-dehydroreticuline
-
-
0.007
NADPH
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 30000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stablilized by NADPH, 1 mM
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 mM NADPH, 50% loss of activity after 30 days
-
4°C, 1 mM NADPH, 50% loss of activity after 20 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
-
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography; recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, the genetic locus, designated STORR [(S)- to (R)-reticuline] encodes both cytochrome P450 and oxidoreductase modules
-
gene PrDRR, genetic map, recombinant expression of His-tagged enzyme in Saccharomyces cerevisiae
-
gene PsDRR1, genetic map, recombinant expression of His-tagged enzyme in Saccharomyces cerevisiae; gene PsDRR1, genetic map, recombinant expression of His-tagged enzyme in Saccharomyces cerevisiae
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
RNAi-mediated silencing of the COR gene family in opium poppy8, and the pTRV2-REPI-a construct targeted a corresponding region in the AKR domain of enzyme PsREPI. Relative REPI transcript abundance is significantly reduced in plants subjected to virus-induced gene silencing using all three constructs as compared to those transformed with empty vector, and the resulting alkaloid profiles are remarkably similar in both the latex and roots