Information on EC 1.14.21.4 - salutaridine synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.21.4
-
RECOMMENDED NAME
GeneOntology No.
salutaridine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-reticuline + NADPH + H+ + O2 = salutaridine + NADP+ + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
morphine biosynthesis
-
-
Isoquinoline alkaloid biosynthesis
-
-
Metabolic pathways
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-
Biosynthesis of secondary metabolites
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-
SYSTEMATIC NAME
IUBMB Comments
(R)-reticuline,NADPH:oxygen oxidoreductase (C-C phenol-coupling)
A heme-thiolate enzyme (P-450). Forms the morphinan alkaloid salutaridine by intramolecular phenol oxidation of reticuline without the incorporation of oxygen into the product.
CAS REGISTRY NUMBER
COMMENTARY hide
149433-84-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
very low activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme silencing causes a profound increase in the absolute accumulation of reticuline at the expense of downstream products, especially morphine
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-norreticuline + NADPH + H+ + O2
norsalutaridine + NADP+ + H2O
show the reaction diagram
(R)-reticuline + NADPH + H+ + O2
salutaridine + NADP+ + H2O
show the reaction diagram
(R)-reticuline + NADPH + O2
salutaridine + NADP+
show the reaction diagram
(R/S)-orientaline
?
show the reaction diagram
-
-
-
-
-
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
(R)-reticuline + NADPH + H+ + O2
salutaridine + NADP+ + H2O
show the reaction diagram
(R)-reticuline + NADPH + O2
salutaridine + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
-
N5-Dinitrophenyl-D-ornithine methyl ester
-
-
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ancymidole
-
-
CO
-
in darkness but not in light
Prochloraz
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.017
(R)-Reticuline
0.15
NADPH
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.027
(R)-Reticuline
Papaver somniferum
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
activity assay
8
-
assay for kinetic analysis
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
about 50% of maximal activity at pH 6.5 and pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay for kinetic analysis
37
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activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 30
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10C: about 30% of maximal activity, 30C: about 65% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
most abundant in carpel
Manually annotated by BRENDA team
-
thebaine-producing
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
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most abundant in stem
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
determined by SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, microsome-bound enzyme, freezing causes a total loss of activity
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-70C, microsome-bound enzyme, 20% loss of activity after 1 month
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22C, microsome-bound enzyme, half-life: 2 h
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in ice water, microsome-bound enzyme, half-life: 20 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
microsomes from insect cells are prepared
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
full-length CYP719B1 cDNA is generated by amplification out of bacterial vector pCR2.1 and inserted into baculovirus transfer vector pVL1392
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