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Information on EC 1.1.1.248 - salutaridine reductase (NADPH)
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1.1.1.248 salutaridine reductase (NADPH)IUBMB Comments
Catalyses the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant.
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The enzyme appears in viruses and cellular organisms
Synonyms
salutaridine reductase, pssar, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
reductase, salutaridine 7-
-
-
-
-
SalR
salutaridine 7-reductase
-
-
-
-
salutaridine reductase
additional information
additional information
the enzyme belongs to the NADPH-dependent short-chain dehydrogenase/reductase family
additional information
the enzyme belongs to the family of short-chain dehydrogenases/reductase
additional information
the enzyme belongs to the family of short-chain dehydrogenases/reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
salutaridinol + NADP+ = salutaridine + NADPH + H+
highly substrate specific transfer of the pro-S hydride, B-type, of NADPH to C-7 of salutaridine
-
salutaridinol + NADP+ = salutaridine + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
salutaridinol:NADP+ 7-oxidoreductase
Catalyses the reversible reduction of salutaridine to salutaridinol, which is a direct precursor of morphinan alkaloids in the poppy plant.
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CAS REGISTRY NUMBER
COMMENTARY
152743-95-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
salutaridine + NAD(P)H + H+
(7S)-salutaridinol + NAD(P)+
NADPH is the highly preferred cofactor, the enzyme shows high substrate specificity, no activity with tropinone, (2)-menthone, codeinone and dehydroreticulinium ion, or nordehydroreticuline. Asp152, Ser180, Tyr236, and Lys240 are involved in the proton transfer system for the reduction of salutaridine, substrate-active site binding structure, overview
the enzyme produces only the (7S)-salutaridinol stereoisomer as product, not the stereoisomer 7-epi-salutaridinol
-
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Papaver arenarium
-
moderate levels of SalR expression in Papaver arenarium
-
-
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
moderate levels of SalR expression in Papaver bracteatum
-
-
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
a step in the unique biosynthesis of morphine via codeine, overview
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-
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
NADPH-dependent reduction of the 7-keto group
no formation of 7-epi-salutaridinol
-
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
-
high levels of SalR expression in all Papaver somniferum varieties
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-
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
-
interaction between SalR and SalAT in morphine biosynthesis
-
-
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
a step in the unique biosynthesis of morphine via codeine, overview
-
-
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
NADPH-dependent reduction of the 7-keto group
no formation of 7-epi-salutaridinol
-
r
salutaridine + NADPH + H+
salutaridinol + NADP+
-
formation of salutaridinol, a precursor for the synthesis of morphine and related opium alkaloids
-
-
?
additional information
?
-
the enzyme is involved in the biosynthesis of morphine
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of morphine
-
-
?
additional information
?
-
interaction of benzylisoquinoline alkaloids with enzymes, modeling, overview
-
-
?
additional information
?
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interaction of benzylisoquinoline alkaloids with enzymes, modeling, overview
-
-
?
additional information
?
-
-
occurrence of active SalR homologue in Papaver pilosum, although it does not produce salutaridine or any other promorphinan alkaloid
-
-
?
additional information
?
-
Papaver pyrenaicum
-
occurrence of active SalR homologue in Papaver pyrenaicum, although it does not produce salutaridine or any other promorphinan alkaloid
-
-
?
additional information
?
-
alkaloid composition of the organism
-
-
?
additional information
?
-
no reduction of 1,2-nordehydroreticuline, 1,2-dehydroreticulinium ion, codeinone, tropinone, or (-)-menthone, no oxidation of (R)-norreticuline, (R)-reticuline, codeine, tropine, or (+)-neomenthol
-
-
?
additional information
?
-
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no reduction of 1,2-nordehydroreticuline, 1,2-dehydroreticulinium ion, codeinone, tropinone, or (-)-menthone, no oxidation of (R)-norreticuline, (R)-reticuline, codeine, tropine, or (+)-neomenthol
-
-
?
additional information
?
-
alkaloid composition of the organism
-
-
?
additional information
?
-
no reduction of 1,2-nordehydroreticuline, 1,2-dehydroreticulinium ion, codeinone, tropinone, or (-)-menthone, no oxidation of (R)-norreticuline, (R)-reticuline, codeine, tropine, or (+)-neomenthol
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
a step in the unique biosynthesis of morphine via codeine, overview
-
-
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
a step in the unique biosynthesis of morphine via codeine, overview
-
-
r
salutaridine + NADPH + H+
salutaridinol + NADP+
-
formation of salutaridinol, a precursor for the synthesis of morphine and related opium alkaloids
-
-
?
additional information
?
-
the enzyme is involved in the biosynthesis of morphine
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of morphine
-
-
?
additional information
?
-
alkaloid composition of the organism
-
-
?
additional information
?
-
alkaloid composition of the organism
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
5% of the activity with NADP+, oxidation reaction, recombinant enzyme
NADH
20% of the activity with NADPH, reduction reaction, recombinant enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
direct influence of a reduction in salAT transcript level by RNAi on the transcription of salR is not evident
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
DNA with apurinic site
pH 9.5, 30°C, recombinant enzyme, oxidation reaction
-
0.031
salutaridine
pH 6.0, 30°C, recombinant enzyme, reduction reaction
additional information
additional information
kinetics, recombinant enzyme
-
additional information
additional information
-
kinetics, recombinant enzyme
-
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7.5
the enzyme shows a steep decrease by 90% of activity within 1.5 pH units on both sides of the optimum at pH 6.0 for the reduction reaction
4.7 - 7.5
sharp increase in activity at pH 4.7, half-maximal activity at pH 7.5, inactive at pH 9.0, recombinant enzyme, reduction reaction
5.8 - 7.8
-
50% of maximal activity at pH 5.8 and at pH 7.8, formation of (7S)-salutaridinol
8.5 - 10
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50% of maximal activity at pH 5.8 and at pH 7.8, formationof salutaridine
9 - 10
maximal activity at pH 9.5, sharp decline in activity at pH 10.0, oxidation reaction, recombinant enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 35
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
recombinant enzyme, 50% of maximal activity at 20°C and 40°C, reduction reaction
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of the short chain dehydrogenase/reductase family of enzymes. The nicotinamide moiety and the substrate-binding pocket are covered by a loop (residues 265-279), on top of which lies a large flap-like domain (residues 105-140). This configuration appears to be a combination of the two common structural themes found in other members of the short chain dehydrogenase/reductase family.
malfunction
-
reduced SalR protein levels correlate with lower morphine levels and a substantial increase in the accumulation of salutaridine. Morphine biosynthesis can be perturbed at each of the six final steps
metabolism
additional information
metabolism
in the biosynthetic pathway for morphine and codeine, salutaridine is reduced to salutaridinol by salutaridine reductase using NADPH as coenzyme
metabolism
-
the enzyme catalyzes a step in the morphinan alkaloid pathway, benzylisoquinoline alkaloid biosynthesis in opium poppy from (R)-reticuline to morphine overview. Morphine biosynthesis can be perturbed at each of the six final steps
additional information
modeling of substrate binding and conformation of bound salutaridine, interactions between SalR and its substrate and coenzyme, overview
additional information
-
modeling of substrate binding and conformation of bound salutaridine, interactions between SalR and its substrate and coenzyme, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SALR_PAPBR
311
0
34055
Swiss-Prot
other Location (Reliability: 2)
SALR_PAPSO
311
0
34050
Swiss-Prot
other Location (Reliability: 3)
A0A2P6PAK4_ROSCH
300
0
32467
TrEMBL
other Location (Reliability: 4)
A0A2P6P783_ROSCH
271
0
29433
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6P760_ROSCH
304
0
33000
TrEMBL
other Location (Reliability: 3)
A0A2P6P753_ROSCH
271
0
29292
TrEMBL
Secretory Pathway (Reliability: 5)
A0A396ITY7_MEDTR
298
0
32820
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6PAK2_ROSCH
300
0
32425
TrEMBL
other Location (Reliability: 4)
A0A2P6PAL0_ROSCH
300
0
32439
TrEMBL
other Location (Reliability: 4)
A0A2P6P749_ROSCH
251
0
27169
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6SGV9_ROSCH
130
0
14548
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34050
1 * 36600, recombinant His-tagged enzyme, SDS-PAGE, 1 * 34050, sequence calculation, the tertiary structure comprises the typical short-chain dehydrogenase/reductase family alpha/beta folding pattern including the four additional helices alphaF-1 to alphaF-4 assumed to prevent the dimerization, modeling and analysis, overview
34100
1 * 34100, sequence calculation, 1 * 40000, recombinant His6-tagged enzyme, SDS-PAGE
36600
1 * 36600, recombinant His-tagged enzyme, SDS-PAGE, 1 * 34050, sequence calculation, the tertiary structure comprises the typical short-chain dehydrogenase/reductase family alpha/beta folding pattern including the four additional helices alphaF-1 to alphaF-4 assumed to prevent the dimerization, modeling and analysis, overview
40000
1 * 34100, sequence calculation, 1 * 40000, recombinant His6-tagged enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1 * 36600, recombinant His-tagged enzyme, SDS-PAGE, 1 * 34050, sequence calculation, the tertiary structure comprises the typical short-chain dehydrogenase/reductase family alpha/beta folding pattern including the four additional helices alphaF'-1 to alphaF'-4 assumed to prevent the dimerization, modeling and analysis, overview
monomer
1 * 34100, sequence calculation, 1 * 40000, recombinant His6-tagged enzyme, SDS-PAGE
monomer
-
1 * 34100, sequence calculation, 1 * 40000, recombinant His6-tagged enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a homology model of the Papaver bracteatum SalR based on the X-ray structure of human carbonyl reductase 1, overview
purified recombinant detagged wild-type and selenomethionine-substituted SalR, hanging drop vapour diffsion method, mixing of 0.002 ml of 6 mg/ml protein in 20 mM Tris buffer, pH 7.5, containing 150 mM NaCl, 5 mM 2-mercaptoethanol, and 4 mM NADPH, with 0.002 ml of reservoir solution containing 0.1 M MES, pH 6.0-6.6, 1.9 M ammonium sulfate, 5% v/v PEG 400, 0.1 M LiCl, and 3% v/v glycerol, 3 weeks, 4°C, X-ray diffraction structure determination and analysis at 1.9 A resolution
to 1.9 A resolution, space group P6422 or P6222. Presence of NADPH is required for crystallization
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F104A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L266A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L266S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L266V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N152A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R44E
site-directed mutagenesis, the mutant enzyme shows altered cofactor specificity and utilizes also NADH in contrast to the wild-type enzyme
R48E
site-directed mutagenesis, the mutant enzyme shows altered cofactor specificity and utilizes also NADH in contrast to the wild-type enzyme
S180A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
V106A
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
D107A
F104A
F104A/I275A
I275A
I275V
the mutant shows altered kinetics compared to the wild-type enzyme
K186V
L185A
L185S
the mutant shows altered kinetics compared to the wild-type enzyme
L185V
the mutant shows altered kinetics compared to the wild-type enzyme
L266A
M271A
N272A
S181A
T182A
V106A
additional information
-
specific virus-induced gene silencing as a functional genomics tool to investigate the regulation of morphine biosynthesis via a systematic reduction in enzyme levels responsible for the final six steps in the pathway, overview. Reduced SalR protein levels correlate with lower morphine levels and a substantial increase in the accumulation of salutaridine
D107A
the mutant shows altered kinetics compared to the wild-type enzyme
F104A
the mutant shows altered kinetics compared to the wild-type enzyme
F104A/I275A
shows no substrate inhibition accompanied by a weak affinity for productive salutaridine binding, kcat is almost 2fold higher compared with the wild-type
F104A/I275A
substitution of Phe104 in the substrate-binding pocket, and Ile275 under the flap domain, the mutant shows altered kinetics compared to the wild-type enzyme
I275A
increase in Km, shows an increase of velocity by a factor of 2.3
I275A
the mutant shows altered kinetics compared to the wild-type enzyme
K186V
moderate effects on substrate affinity, exhibits a turnover number similar to that of the wild-type
K186V
the mutant shows altered kinetics compared to the wild-type enzyme
L185A
the mutant shows altered kinetics compared to the wild-type enzyme
L266A
the mutant shows altered kinetics compared to the wild-type enzyme
M271A
the mutant shows altered kinetics compared to the wild-type enzyme
N272A
the mutant shows altered kinetics compared to the wild-type enzyme
S181A
moderate effects on substrate affinity, increase in kcat by 50%
S181A
the mutant shows altered kinetics compared to the wild-type enzyme
T182A
the mutant shows altered kinetics compared to the wild-type enzyme
V106A
moderate effects on substrate affinity, increase in kcat by 90%
V106A
the mutant shows altered kinetics compared to the wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
SalR is susceptible to inactivation and soluble aggregation in an oxidative environment
storage of purified at 193 K without 2-mercaptoethanol results in complete loss of activity. Inactive enzyme regains activity on incubation overnight at 277 K with 2-mercaptoethanol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by cobalt affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain SG13009
recombinant N-terminally His-tagged wild-type and selenomethionine-substituted SalR from Escherichia coli by cobalt affinity chromatography, cleavage of the N-terminal His-tag by thrombin, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the pMyr vector and expressed as fusion protein with a myristylation sequence, which anchors the target protein to the yeast membrane. Fusion proteins (pSOS/SalAT and pMyr/SalR) coexpressed in the Saccharomyces cerevisiae cdc25H strain. SalR amplified from the recombinant plasmid SalR/pQE-30. The 0.9-kb DNA fragment ligated into an NheI/EcoRI-digested pET28a expression vector. SalR/pET28a expression construct transformed into Escherichia coli BL21(DE3)RIL
-
gene salR, DNA and amino acid sequence determination and analysis, expression profile, overexpression in Escherichia coli strain SG13009 as His6-tagged enzyme
gene salR, expression of N-terminally His-tagged enzyme in Escherichia coli, a selenomethionine-substituted SalR is produced by inhibition of the methionine biosynthetic pathway with the same expression vector and Escherichia coli strain used for expression of wild-type SalR
salR, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli
salutaridine synthase (PsSAS), salutaridine reductase (PsSAR) and salutaridinol acetyltransferase (PsSAT) are functionally coexpressed in Saccharomyces cerevisiae and optimization of the pH conditions allowed for productive spontaneous rearrangement of salutaridinol-7-O-acetate and synthesis of thebaine from (R)-reticuline. A 7-gene pathway for the production of codeine and morphine from (R)-reticuline is reconstituted. Yeast cell feeding assays using (R)-reticuline, salutaridine or codeine as substrates show that all enzymes are functionally coexpressed in yeast and that activity of salutaridine reductase and codeine-O-demethylase likely limit flux to morphine synthesis. The results of this study describe a significant advance for the synthesis of morphinans in Saccharomyces cerevisiae and pave the way for their complete synthesis in recombinant microbes
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
storage of purified at 193 K without 2-mercaptoethanol results in complete loss of activity. Inactive enzyme regains activity on incubation overnight at 277 K with 2-mercaptoethanol
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
KP400665
the Papaper somniferum enzymes salutaridine synthase (SAS), salutaridine reductase (SAR) and salutaridinol acetyltransferase (SAT) are functionally co-expressed in Saccharomyces cerevisiae and optimization of the pH conditions allows for productive spontaneous rearrangement of salutaridinol-7-O-acetate and synthesis of thebaine from (R)-reticuline. Upon reconstitution of a 7-gene pathway for the production of codeine and morphine from (R)-reticuline, activity of salutaridine reductase and codeine-O-demethylase likely limit flux to morphine synthesis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gerardy, R.; Zenk, M.H.
Purification and characterization of salutaridine:NADPH 7-oxidoreductase from Papaver somniferum
Phytochemistry
34
125-132
1993
no activity in Papaver alpinum, no activity in Papaver atlanticum, no activity in Papaver dubium, no activity in Papaver feddei, no activity in Papaver lateritium, no activity in Papaver oreophilum, no activity in Papaver orientale, no activity in Papaver persicum, no activity in Papaver pilosum, no activity in Papaver rhoeas, no activity in Papaver rupifragum, no activity in Papaver strigosum, no activity in Papaver tauricula, no activity in Papaver triniifolium, Papaver bracteatum, Papaver somniferum
-
brenda
Ziegler, J.; Voigtlaender, S.; Schmidt, J.; Kramell, R.; Miersch, O.; Ammer, C.; Gesell, A.; Kutchan, T.M.
Comparative transcript and alkaloid profiling in Papaver species identifies a short chain dehydrogenase/reductase involved in morphine biosynthesis
Plant J.
48
177-192
2006
Papaver somniferum (Q071N0), Papaver somniferum, Papaver somniferum salR (Q071N0)
brenda
Geissler, R.; Brandt, W.; Ziegler, J.
Molecular modeling and site-directed mutagenesis reveal the benzylisoquinoline binding site of the short-chain dehydrogenase/reductase salutaridine reductase
Plant Physiol.
143
1493-1503
2007
Papaver bracteatum (A4UHT7), Papaver bracteatum
brenda
Ziegler, J.; Brandt, W.; Geissler, R.; Facchini, P.J.
Removal of substrate inhibition and increase in maximal velocity in the short chain dehydrogenase/reductase salutaridine reductase involved in morphine biosynthesis
J. Biol. Chem.
284
26758-26767
2009
Papaver somniferum (Q071N0)
brenda
Ziegler, J.; Facchini, P.J.; Geissler, R.; Schmidt, J.; Ammer, C.; Kramell, R.; Voigtlaender, S.; Gesell, A.; Pienkny, S.; Brandt, W.
Evolution of morphine biosynthesis in opium poppy
Phytochemistry
70
1696-1707
2009
Papaver somniferum, Papaver arenarium, Papaver pilosum, Papaver pyrenaicum, Papaver bracteatum (A4UHT7)
brenda
Kempe, K.; Higashi, Y.; Frick, S.; Sabarna, K.; Kutchan, T.M.
RNAi suppression of the morphine biosynthetic gene salAT and evidence of association of pathway enzymes
Phytochemistry
70
579-589
2009
Papaver somniferum
brenda
Higashi, Y.; Smith, T.J.; Jez, J.M.; Kutchan, T.M.
Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum
Acta Crystallogr. Sect. F
66
163-166
2010
Papaver somniferum (Q071N0), Papaver somniferum
brenda
Wijekoon, C.P.; Facchini, P.J.
Systematic knockdown of morphine pathway enzymes in opium poppy using virus-induced gene silencing
Plant J.
69
1052-1063
2012
Papaver somniferum
brenda
Higashi, Y.; Kutchan, T.M.; Smith, T.J.
Atomic structure of salutaridine reductase from the opium poppy (Papaver somniferum)
J. Biol. Chem.
286
6532-6541
2011
Papaver somniferum (Q071N0), Papaver somniferum
brenda
Fossati, E.; Narcross, L.; Ekins, A.; Falgueyret, J.P.; Martin, V.J.
Synthesis of morphinan alkaloids in Saccharomyces cerevisiae
PLoS ONE
10
e0124459
2015
Papaver somniferum (KP400665), Papaver somniferum
brenda
Fossati, E.; Narcross, L.; Ekins, A.; Falgueyret, J.P.; Martin, V.J.
Synthesis of morphinan alkaloids in Saccharomyces cerevisiae
PLoS ONE
10
e0124459
2015
Papaver somniferum (Q071N0), Papaver somniferum
brenda
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