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Information on EC 1.1.3.16 - ecdysone oxidase
for references in articles please use BRENDA:EC1.1.3.16
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.16 ecdysone oxidase
IUBMB Comments
2,6-Dichloroindophenol can act as an acceptor.
The enzyme appears in viruses and cellular organisms
- 1.1.3.16
- ecdysteroids
- 3-dehydroecdysone
- midgut
-
molting
- silkworm
-
instar
- larval
- 20-hydroxyecdysone
-
spodoptera
-
metamorphosis
- lepidoptera
- littoralis
- ecdysterone
- hemolymph
-
prothoracic
- manduca
-
3beta-hydroxysteroid
- sexta
- leafworm
-
beta-reductase
- pupae
-
fifth-instar
-
glucose-methanol-choline
- blowfly
-
malpighian
-
alpha-hydroxy
-
cis-regulatory
-
oxygen-dependent
- hornworm
-
hemocytes
-
larval-pupal
- calliphora
-
silk
-
nadp-binding
showSynonyms
ecdysone oxidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-ecdysone oxidase
-
-
-
-
oxidase, ecdysone
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ecdysone + O2 = 3-dehydroecdysone + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
ecdysteroid metabolism (arthropods)
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SYSTEMATIC NAME
IUBMB Comments
ecdysone:oxygen 3-oxidoreductase
2,6-Dichloroindophenol can act as an acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
56803-12-4
-
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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
2-deoxy-20-hydroxyecdysone + O2
3-dehydro-2-deoxy-20-hydroxyecdysone + H2O2
-
Substrates: -
Products: -
Products: -
?
2-deoxyecdysone + O2
3-dehydro-2-deoxyecdysone + H2O2
-
Substrates: -
Products: -
Products: -
?
5,20-dihydroxyecdysone + O2
3-dehydro-5,20-dihydroxyecdysone + H2O2
-
Substrates: -
Products: -
Products: -
?
cyasterone + O2
3-dehydrocyasterone + H2O2
-
Substrates: -
Products: -
Products: -
?
ecdysone + oxidized 2,6-dichloroindophenol
3-dehydroecdysone + reduced 2,6-dichloroindophenol
inokosterone + O2
3-dehydroinokosterone + H2O2
-
Substrates: -
Products: -
Products: -
?
makisterone + O2
3-dehydromakisterone + H2O2
-
Substrates: -
Products: -
Products: -
?
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
Substrates: -
Products: -
Products: -
?
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
Substrates: probably part of the catabolic system that inactivates the molting hormones
Products: -
Products: -
?
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
Substrates: -
Products: -
Products: -
?
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
Substrates: first step in reaction sequence for the conversion of ecdysone and 20-hydroxyecdysone to their 3(alpha)-epimers
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
Substrates: inactivation of ecdysone
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: artificial electron acceptors in vitro in ascending order: ferricyanide, methylene blue, 2,6-dichloroindophenol, 5-methazine methyl sulfate
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: artificial electron acceptors in vitro in ascending order: ferricyanide, methylene blue, 2,6-dichloroindophenol, 5-methazine methyl sulfate
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: 2,6-dichloroindophenol can act as acceptor
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: 2,6-dichloroindophenol can act as acceptor
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: FAD, NAD+, NADP+, and FMN can serve as hydrogen acceptors
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: probably part of the catabolic system that inactivates the molting hormones
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: -
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: first step in reaction sequence for the conversion of ecdysone and 20-hydroxyecdysone to their 3(alpha)-epimers
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: -
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
Substrates: -
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
Products: i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + oxidized 2,6-dichloroindophenol
3-dehydroecdysone + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
r
ecdysone + oxidized 2,6-dichloroindophenol
3-dehydroecdysone + reduced 2,6-dichloroindophenol
-
Substrates: 163% activity compared to O2
Products: -
Products: -
r
ecdysteroids + O2
3-dehydroecdysteroids + H2O2
-
Substrates: -
Products: -
Products: -
?
ecdysteroids + O2
3-dehydroecdysteroids + H2O2
-
Substrates: structural requirements: alpha,beta-unsaturated keto function at C-6 and several hydroxyl functions including the hydroxyls at C-3 and at C-22
Products: -
Products: -
?
ecdysteroids + O2
3-dehydroecdysteroids + H2O2
-
Substrates: -
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
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
Substrates: probably part of the catabolic system that inactivates the molting hormones
Products: -
Products: -
?
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
Substrates: first step in reaction sequence for the conversion of ecdysone and 20-hydroxyecdysone to their 3(alpha)-epimers
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
Substrates: inactivation of ecdysone
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: probably part of the catabolic system that inactivates the molting hormones
Products: -
Products: -
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
Substrates: first step in reaction sequence for the conversion of ecdysone and 20-hydroxyecdysone to their 3(alpha)-epimers
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methanol
-
31% inhibition at 0.5%, 62% inhibition at 10%, 90% inhibition at 20%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activities in different larval, pupal and adult stages
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3 - 8.6
-
pH 5.3: about 85% of activity maximum, pH 8.6: about 15% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
during metamorphosis, expression is significantly high in malpighian tubules in comparison to salivary glands
brenda
during metamorphosis, expression is significantly high in malpighian tubules in comparison to salivary glands
brenda
additional information
-
no detectable expression is found in the midgut or silk gland
brenda
-
the enzyme is predominantly expressed in the midgut during the early pupal stage
brenda
-
expression level in testis is about five-fold higher than that in hemocyte
brenda
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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
malfunction
-
enzyme deletion extends the duration of the final instar larval stage
metabolism
ecdysone is inactivated to 3-dehydroecdysone under ecdysone oxidase, followed by NAD(P)H-dependent irreversible reduction to 3-epiecdysteroid under 3-dehydroecdysone 3alpha-reductase. On the other hand, 3-dehydroecdysone undergoes reversible reduction to ecdysone by 3-dehydroecdysone 3beta-reductase in the hemolymph
physiological function
-
middle silk gland-specific enzyme overexpression inhibits autophagy in the silk gland
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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). EO_BOMMO
668
0
72596
Swiss-Prot
Secretory Pathway (Reliability: 5)
EO_DROME
657
1
72560
Swiss-Prot
Secretory Pathway (Reliability: 3)
EO_SPOLI
599
1
65207
Swiss-Prot
other Location (Reliability: 5)
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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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to precipitation with ammonium sulfate and redissolvation or dialysis
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
into the pSI expression vector for transfection of COS-7 cells, and into the pGEM-T vector, used as templates to construct standard curves
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in presence of ecdysone, there is significant upregulation of ecdysone oxidase in malpighian tubules in comparison to salivary gland
the expression of the enzyme gene is elevated at 0.5 h after treatment with ecdysone, and reaches a peak at 1 h after treatment, and then decreases to normal level at next time points
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weinrich, G.F.; Thompson, M.J.; Svoboda, J.A.
Ecdysone oxidase and 3-oxoecdysteroid reductases in Manduca sexta midgut: kinetic parameters
Arch. Insect Biochem. Physiol.
12
201-218
1989
Manduca sexta
-
brenda
Milner, N.P.; Rees, H.H.
Involvement of 3-dehydroecdysone in the 3-epimerization of ecdysone
Biochem. J.
231
369-374
1985
Spodoptera littoralis
brenda
Koolman, J.
Ecdysone oxidase
Methods Enzymol.
111
419-429
1985
Aeshna cyanea, Calliphora vicina, Choristoneura fumiferana, Drosophila hydei, Drosophila melanogaster, Gryllus bimaculatus, Locusta migratoria, Tenebrio molitor
-
brenda
Blais, C.; Lafont, R.
Ecdysteroid metabolism by soluble enzymes from an insect. Metabolic relationships between 3beta-hydroxy-, 3alpha-hydroxy- and 3-oxoecdysteroids
Hoppe-Seyler's Z. Physiol. Chem.
365
809-817
1984
Pieris brassicae
brenda
Koolman, J.
Ecdysone oxidase in insects
Hoppe-Seyler's Z. Physiol. Chem.
359
1315-1321
1978
Calliphora vicina, Daphnis nerii, Drosophila melanogaster, Periplaneta americana
brenda
Koolman, J.; Karlson, P.
Ecdysone oxidase: reaction and specificity
Eur. J. Biochem.
89
453-460
1978
Calliphora vicina
brenda
Koolman, J.; Karlson, P.
Ecdysone Oxidase, an enzyme from the blowfly Calliphora erythrocephala (Meigen)
Hoppe-Seyler's Z. Physiol. Chem.
356
1131-1138
1975
Calliphora vicina
brenda
Chen, J.H.; Powls, R.; Rees, H.H.; Wilkinson, M.C.
Purification of ecdysone oxidase and 3-dehydroecdysone 3-alpha-reductase from the cotton leafworm, Spodoptera littoralis
Insect Biochem. Mol. Biol.
29
899-908
1999
Spodoptera littoralis
-
brenda
Takeuchi, H.; Chen, J.H.; O'Reilly, D.R.; Turner, P.C.; Rees, H.H.
Regulation of ecdysteroid signaling: cloning and characterization of ecdysone oxidase. A novel steroid oxidase from the cotton leafworm, Spodoptera littoralis
J. Biol. Chem.
276
26819-26828
2001
Spodoptera littoralis (Q95NZ0), Spodoptera littoralis
brenda
Weirich, G.F.; Feldlaufer, M.F.; Svoboda, J.A.
Ecdysone oxidase and 3-oxoecdysteroid reductases in Manduca sexta: developmental changes and tissue distribution