Information on EC 1.14.21.4 - salutaridine synthase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.21.4
-
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RECOMMENDED NAME
GeneOntology No.
salutaridine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-reticuline + NADPH + H+ + O2 = salutaridine + NADP+ + 2 H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Isoquinoline alkaloid biosynthesis
-
-
Metabolic pathways
-
-
morphine biosynthesis
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY hide
149433-84-1
-
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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
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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
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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
-
-
-
-
-
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
-
N5-Dinitrophenyl-D-ornithine methyl ester
-
-
NADPH
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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
-
-
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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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
about 50% of maximal activity at pH 6.5 and pH 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay for kinetic analysis
37
-
activity assay
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 30
-
10°C: about 30% of maximal activity, 30°C: about 65% of maximal activity
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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
-
most abundant in stem
Manually annotated by BRENDA team
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
-
x * 56000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, microsome-bound enzyme, freezing causes a total loss of activity
-
-70°C, microsome-bound enzyme, 20% loss of activity after 1 month
-
22°C, microsome-bound enzyme, half-life: 2 h
-
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.21.4)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)