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Information on EC 1.14.13.101 - senecionine N-oxygenase
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1.14.13.101 senecionine N-oxygenaseIUBMB Comments
A flavoprotein. NADH cannot replace NADPH. While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates . Senecionine N-oxide is used by insects as a chemical defense: senecionine N-oxide is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P-450 oxidase when absorbed by insectivores.
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The enzyme appears in viruses and cellular organisms
Synonyms
senecionine n-oxygenase, pa n-oxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
senecionine + NADPH + H+ + O2 = senecionine N-oxide + NADP+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N-oxidation
oxidation
redox reaction
reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
senecionine,NADPH:oxygen oxidoreductase (N-oxide-forming)
A flavoprotein. NADH cannot replace NADPH. While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates [1]. Senecionine N-oxide is used by insects as a chemical defense: senecionine N-oxide is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P-450 oxidase when absorbed by insectivores.
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CAS REGISTRY NUMBER
COMMENTARY
220581-68-0
-
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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
atropine + NADPH + O2
atropine N-oxide + NADP+ + H2O
21% of the activity with monocrotaline
-
?
axillaridine + NADPH + H+ + O2
axillaridine N-oxide + NADP+ + H2O
-
-
-
?
monocrotaline + NADPH + H+ + O2
monocrotaline N-oxide + NADP+ + H2O
-
-
-
?
phalaenopsine + NADPH + H+ + O2
phalaenopsine N-oxide + NADP+ + H2O
-
-
-
?
phalaenopsine + NADPH + O2
phalaenopsine N-oxide + NADP+ + H2O
19% of the activity with monocrotaline
-
?
retronecine + NADPH + H+ + O2
retronecine N-oxide + NADP+ + H2O
-
-
-
?
seneciphylline + NADPH + H+ + O2
seneciphylline N-oxide + NADP+ + H2O
-
second best substrate
-
?
senecivernine + NADPH + H+ + O2
senecivernine N-oxide + NADP+ + H2O
-
-
-
?
triangularine + NADPH + O2
triangularine N-oxide + NADP+ + H2O
-
60% of the activity with senecionine
-
?
axillaridine + NADPH + O2
axillaridine N-oxide + NADP+ + H2O
-
79% of the activity with senecionine
-
?
axillaridine + NADPH + O2
axillaridine N-oxide + NADP+ + H2O
-
93% of the activity with senecionine
-
?
axillaridine + NADPH + O2
axillaridine N-oxide + NADP+ + H2O
-
76% of the activity with senecionine
-
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
69% of the activity with monocrotaline
-
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
-
55% of the activity with senecionine
-
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
-
38% of the activity with senecionine
-
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
-
74% of the activity with senecionine
-
?
axillarine + NADPH + O2
axillarine N-oxide + NADP+ + H2O
74% of the activity with senecionine, native enzyme. 83% of the activity with senecionine, recombinant enzyme
-
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
49% of the activity with monocrotaline
-
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
-
86% of the activity with senecionine
-
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
-
115% of the activity with senecionine
-
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
-
25% of the activity with senecionine
-
?
heliotrine + NADPH + O2
heliotrine N-oxide + NADP+ + H2O
25% of the activity with senecionine, native enzyme. 49% of the activity with senecionine, recombinant enzyme
-
?
indicine + NADPH + O2
indicine N-oxide + NADP+ + H2O
-
90% of the activity with senecionine
-
?
indicine + NADPH + O2
indicine N-oxide + NADP+ + H2O
-
78% of the activity with senecionine
-
?
indicine + NADPH + O2
indicine N-oxide + NADP+ + H2O
-
35% of the activity with senecionine
-
?
lycopsamine + NADPH + O2
lycopsamine N-oxide + NADP+ + H2O
-
93% of the activity with senecionine
-
?
lycopsamine + NADPH + O2
lycopsamine N-oxide + NADP+ + H2O
-
75% of the activity with senecionine
-
?
lycopsamine + NADPH + O2
lycopsamine N-oxide + NADP+ + H2O
-
20% of the activity with senecionine
-
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
-
-
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
-
103% of the activity with senecionine
-
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
-
110% of the activity with senecionine
-
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
-
92% of the activity with senecionine
-
?
monocrotaline + NADPH + O2
monocrotaline N-oxide + NADP+ + H2O
92% of the activity with senecionine, native enzyme. 94% of the activity with senecionine, recombinant enzyme
-
?
retrorsine + NADPH + O2
retrorsine N-oxide + NADP+ + H2O
-
as active as senecionine
-
?
retrorsine + NADPH + O2
retrorsine N-oxide + NADP+ + H2O
-
93% of the activity with senecionine
-
?
retrorsine + NADPH + O2
retrorsine N-oxide + NADP+ + H2O
-
97% of the activity with senecionine
-
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
43% of the activity with monocrotaline
-
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
-
79% of the activity with senecionine
-
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
-
81% of the activity with senecionine
-
?
rinderine + NADPH + O2
rinderine N-oxide + NADP+ + H2O
-
23% of the activity with senecionine
-
?
senecionine + NADPH + H+ + O2
senecionine N-oxide + NADP+ + H2O
-
-
-
?
senecionine + NADPH + H+ + O2
senecionine N-oxide + NADP+ + H2O
-
most efficient substrate
-
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
61% of the activity with monocrotaline
-
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
-
-
-
?
senecionine + NADPH + O2
senecionine N-oxide + NADP+ + H2O
-
-
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
59% of the activity with monocrotaline
-
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
-
117% of the activity with senecionine
-
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
-
119% of the activity with senecionine
-
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
-
95% of the activity with senecionine
-
?
seneciphylline + NADPH + O2
seneciphylline N-oxide + NADP+ + H2O
95% of the activity with senecionine, native enzyme. 93% of the activity with senecionine, recombinant enzyme
-
?
senecivernine + NADPH + O2
senecivernine N-oxide + NADP+ + H2O
-
107% of the activity with senecionine
-
?
senecivernine + NADPH + O2
senecivernine N-oxide + NADP+ + H2O
-
113% of the activity with senecionine
-
?
senecivernine + NADPH + O2
senecivernine N-oxide + NADP+ + H2O
-
81% of the activity with senecionine
-
?
additional information
?
-
the enzyme shows activity with glutathione (41% of the activity with monocrotaline)
-
?
additional information
?
-
-
the enzyme shows activity with glutathione (41% of the activity with monocrotaline)
-
?
additional information
?
-
-
the enzyme N-oxidizes only alkaloids with structural elements which are essential for hepatotoxic and genotoxic pyrrolizidine alkaloids, i.e. 1,2-double bond, esterification of the allylic hydroxyl group, presence of a second free or esterified hydroxyl group at carbon 7. No activity with: triangularine, senkirkine, sarracine, supinine, phalaenopsine, retronecine, heliotridine, supinidine, isoretronecanol, nicotine, caffeine, tropane alkaloids, quinolizidine alkaloids, indole alkaloids, isoquinolines and synthetic heterocyclic tertiary amines
-
?
additional information
?
-
-
the enzyme N-oxidizes only alkaloids with structural elements which are essential for hepatotoxic and genotoxic pyrrolizidine alkaloids, i.e. 1,2-double bond, esterification of the allylic hydroxyl group, presence of a second free or esterified hydroxyl group at carbon 7. No activity with: triangularine, senkirkine, sarracine, supinine, phalaenopsine, retronecine, heliotridine, supinidine, isoretronecanol, nicotine, caffeine, tropane alkaloids, quinolizidine alkaloids, indole alkaloids, isoquinolines and synthetic heterocyclic tertiary amines
-
?
additional information
?
-
the enzyme is highly specific for toxic pyrrolizidine alkaloids. No activity with: senkirkine, dimethylaniline, L-Pro, caffeine, atropine, supinidine, retronecine, phalaenopsine
-
?
additional information
?
-
-
the enzyme is highly specific for toxic pyrrolizidine alkaloids. No activity with: senkirkine, dimethylaniline, L-Pro, caffeine, atropine, supinidine, retronecine, phalaenopsine
-
?
additional information
?
-
-
the enzyme N-oxidizes only alkaloids with structural elements which are essential for hepatotoxic and genotoxic pyrrolizidine alkaloids, i.e. 1,2-double bond, esterification of the allylic hydroxyl group, presence of a second free or esterified hydroxyl group at carbon 7. No activity with: senkirkine, sarracine, supinine, phalaenopsine, retronecine, heliotridine, supinidine, isoretronecanol, nicotine, caffeine, tropane alkaloids, quinolizidine alkaloids, indole alkaloids, isoquinolines and synthetic heterocyclic tertiary amines
-
?
additional information
?
-
the enzyme allows the larvae to feed on pyrrolizidine alkaloid-containing plants and to accumulate predation-deterrent pyrrolizidine alkaloids in the hemolymph
-
?
additional information
?
-
-
the enzyme allows the larvae to feed on pyrrolizidine alkaloid-containing plants and to accumulate predation-deterrent pyrrolizidine alkaloids in the hemolymph
-
?
additional information
?
-
-
no activity with senkirkine, heliotridine, supinidine, ephedrine, dimethylaniline, L-cysteine, hydroxylamine, and glutathione
-
?
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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
senecionine + NADPH + H+ + O2
senecionine N-oxide + NADP+ + H2O
-
most efficient substrate
-
-
?
seneciphylline + NADPH + H+ + O2
seneciphylline N-oxide + NADP+ + H2O
-
second best substrate
-
-
?
additional information
?
-
the enzyme allows the larvae to feed on pyrrolizidine alkaloid-containing plants and to accumulate predation-deterrent pyrrolizidine alkaloids in the hemolymph
-
?
additional information
?
-
-
the enzyme allows the larvae to feed on pyrrolizidine alkaloid-containing plants and to accumulate predation-deterrent pyrrolizidine alkaloids in the hemolymph
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
n-octylamine
-
activity of solubilized enzyme is 1.6fold increased by 0.5 mM n-octylamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
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
-
in potassium phosphate buffer (10 mM), Tris/HCl buffer (10 mM), and in glycine/NaOH buffer (100 mM)
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 45
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
-
determination on an Ampholine PAGplate pH 3.5-9.5 using a horizantal electrophoresis system
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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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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). SNO1_TYRJA
456
0
52232
Swiss-Prot
Secretory Pathway (Reliability: 2)
D6CHF1_DIASN
395
0
45588
TrEMBL
other Location (Reliability: 2)
D6CHF3_ESTAC
396
0
45694
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
20 min, solubilized enzyme is completely inactivated in absence of NADPH, preincubation the presence of NADPH has no effect
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressing GgPNO without the signal peptide in at least a partially soluble and active form. Betaine is added to the medium and promotes its uptake by osmotic stress by sorbitol. Further improvements are achieved by coexpression with the Escherichia coli chaperones DnaK/DnaJ/GrpE by using the plasmid pRDKJG and by reducing the expression temperature to 4°C
the heterologous expression results in the formation of an insoluble and inactive protein. Despite the finding that protein solubilization and subsequent renaturation results in an active protein, the specific activity remains low. Active SNO is detected by using an an Sf9 insect cell expression system, but the yield of protein is too low for further biochemical characterization. Using an alignment of senecionine N-oxygenase of Tyria jacobaeae and of flavin-dependent monooxygenase-like sequences of the dipteran species Drosophila melanogaster and Anopheles gambiae, several new flavin-dependent monooxygenase sequences of arctiids and other Lepidoptera are idenified
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lindigkeit, R.; Biller, A.; Buch, M.; Schiebel, H.M.; Boppre, M.; Hartmann, T.
The two faces of pyrrolizidine alkaloids: the role of the tertiary amine and its N-oxide in chemical defense of insects with aquired alkaloids
Eur. J. Biochem.
245
626-636
1997
Arctia caja, Tyria jacobaeae, no activity in Spodoptera littoralis, Creatonotos transiens, Callimorpha dominula, Arctia intercalaris, Amerila phaedra, Idea leuconoe, Zonocerus variegatus
brenda
Naumann, C.; Hartmann, T.; Ober, D.
Evolutionary recruitment of a flavin-dependent monooxygenase for the detoxification of host plant-defended arctiid moth Tyria jacobaeae
Proc. natl. Acad. Sci. USA
99
6085-6090
2002
Tyria jacobaeae (Q8MP06), Tyria jacobaeae
brenda
Chang, A.; Hartmann, T.
Solubilization and characterization of a senecionine N-oxygenase from Crotalaria scassellatii seedlings
Phytochemistry
49
1859-1866
1998
Crotalaria scassellatii
-
brenda
Sehlmeyer, S.; Wang, L.; Langel, D.; Heckel, D.G.; Mohagheghi, H.; Petschenka, G.; Ober, D.
Flavin-dependent monooxygenases as a detoxification mechanism in insects: new insights from the arctiids (lepidoptera)
PLoS ONE
5
e10435
2010
Apantesis nevadensis geneura (D6CHF2), Apantesis nevadensis geneura, Tyria jacobaeae (Q8MP06), Tyria jacobaeae
brenda
Wang, L.; Beuerle, T.; Timbilla, J.; Ober, D.
Independent recruitment of a flavin-dependent monooxygenase for safe accumulation of sequestered pyrrolizidine alkaloids in grasshoppers and moths
PLoS ONE
7
e31796
2012
Zonocerus variegatus
brenda
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