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Information on EC 1.1.1.248 - salutaridine reductase (NADPH)
for references in articles please use BRENDA:EC1.1.1.248
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
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.
The enzyme appears in viruses and cellular organisms
showSynonyms
salutaridine reductase, pssar, more
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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
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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
MetaCyc
morphine biosynthesis
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
salutaridine + NAD(P)H + H+
(7S)-salutaridinol + NAD(P)+
Substrates: 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
Products: the enzyme produces only the (7S)-salutaridinol stereoisomer as product, not the stereoisomer 7-epi-salutaridinol
Products: the enzyme produces only the (7S)-salutaridinol stereoisomer as product, not the stereoisomer 7-epi-salutaridinol
r
salutaridine + NADH + H+
salutaridinol + NAD+
Substrates: -
Products: -
Products: -
r
salutaridinol + NADP+
salutaridine + NADPH + H+
Substrates: -
Products: -
Products: -
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Papaver arenarium
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Substrates: moderate levels of SalR expression in Papaver arenarium
Products: -
Products: -
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: -
Products: -
Products: -
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: moderate levels of SalR expression in Papaver bracteatum
Products: -
Products: -
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: -
Products: -
Products: -
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
-
Substrates: r
Products: -
Products: -
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: a step in the unique biosynthesis of morphine via codeine, overview
Products: -
Products: -
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: NADPH-dependent reduction of the 7-keto group
Products: no formation of 7-epi-salutaridinol
Products: no formation of 7-epi-salutaridinol
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
-
Substrates: high levels of SalR expression in all Papaver somniferum varieties
Products: -
Products: -
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
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Substrates: interaction between SalR and SalAT in morphine biosynthesis
Products: -
Products: -
?
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: a step in the unique biosynthesis of morphine via codeine, overview
Products: -
Products: -
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: NADPH-dependent reduction of the 7-keto group
Products: no formation of 7-epi-salutaridinol
Products: no formation of 7-epi-salutaridinol
r
salutaridine + NADPH + H+
salutaridinol + NADP+
-
Substrates: -
Products: -
Products: -
r
salutaridine + NADPH + H+
salutaridinol + NADP+
Substrates: -
Products: -
Products: -
r
salutaridine + NADPH + H+
salutaridinol + NADP+
-
Substrates: formation of salutaridinol, a precursor for the synthesis of morphine and related opium alkaloids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the biosynthesis of morphine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the biosynthesis of morphine
Products: -
Products: -
?
additional information
?
-
Substrates: interaction of benzylisoquinoline alkaloids with enzymes, modeling, overview
Products: -
Products: -
?
additional information
?
-
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Substrates: interaction of benzylisoquinoline alkaloids with enzymes, modeling, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: occurrence of active SalR homologue in Papaver pilosum, although it does not produce salutaridine or any other promorphinan alkaloid
Products: -
Products: -
?
additional information
?
-
Papaver pyrenaicum
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Substrates: occurrence of active SalR homologue in Papaver pyrenaicum, although it does not produce salutaridine or any other promorphinan alkaloid
Products: -
Products: -
?
additional information
?
-
Substrates: alkaloid composition of the organism
Products: -
Products: -
?
additional information
?
-
-
Substrates: alkaloid composition of the organism
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: alkaloid composition of the organism
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: -
Products: -
Products: -
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: a step in the unique biosynthesis of morphine via codeine, overview
Products: -
Products: -
r
salutaridine + NADPH + H+
(7S)-salutaridinol + NADP+
Substrates: a step in the unique biosynthesis of morphine via codeine, overview
Products: -
Products: -
r
salutaridine + NADPH + H+
salutaridinol + NADP+
-
Substrates: -
Products: -
Products: -
r
salutaridine + NADPH + H+
salutaridinol + NADP+
Substrates: -
Products: -
Products: -
r
salutaridine + NADPH + H+
salutaridinol + NADP+
-
Substrates: formation of salutaridinol, a precursor for the synthesis of morphine and related opium alkaloids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the biosynthesis of morphine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the biosynthesis of morphine
Products: -
Products: -
?
additional information
?
-
Substrates: alkaloid composition of the organism
Products: -
Products: -
?
additional information
?
-
-
Substrates: alkaloid composition of the organism
Products: -
Products: -
?
additional information
?
-
Substrates: alkaloid composition of the organism
Products: -
Products: -
?
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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, 30Ā°C, recombinant enzyme, oxidation reaction
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0.031
salutaridine
pH 6.0, 30Ā°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 20Ā°C and 40Ā°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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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