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Information on EC 1.1.1.248 - salutaridine reductase (NADPH) and Organism(s) Papaver bracteatum and UniProt Accession A4UHT7
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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 taxonomic range for the selected organisms is: Papaver bracteatum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
salutaridine reductase, pssar, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
reductase, salutaridine 7-
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-
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salutaridine 7-reductase
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-
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additional information
the enzyme belongs to the NADPH-dependent short-chain dehydrogenase/reductase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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reduction
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-
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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.
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
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r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
moderate levels of SalR expression in Papaver bracteatum
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-
?
additional information
?
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the enzyme is involved in the biosynthesis of morphine
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?
additional information
?
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the enzyme is involved in the biosynthesis of morphine
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?
additional information
?
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interaction of benzylisoquinoline alkaloids with enzymes, modeling, overview
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?
additional information
?
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interaction of benzylisoquinoline alkaloids with enzymes, modeling, overview
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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
additional information
?
-
the enzyme is involved in the biosynthesis of morphine
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-
?
additional information
?
-
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the enzyme is involved in the biosynthesis of morphine
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
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additional information
additional information
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kinetics of wild-type and mutant enzymes, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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)
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by cobalt affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
salR, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli
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
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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
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 arenarium, Papaver bracteatum (A4UHT7), Papaver pilosum, Papaver pyrenaicum, Papaver somniferum
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