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Information on EC 1.1.3.16 - ecdysone oxidase
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EC Tree
1.1.3.16 ecdysone oxidaseIUBMB Comments
2,6-Dichloroindophenol can act as an acceptor.
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Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
ecdysone oxidase, 
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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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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
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
5,20-dihydroxyecdysone + O2
3-dehydro-5,20-dihydroxyecdysone + H2O2
-
-
-
-
?
ecdysone + oxidized 2,6-dichloroindophenol
3-dehydroecdysone + reduced 2,6-dichloroindophenol
2-deoxy-20-hydroxyecdysone + O2
3-dehydro-2-deoxy-20-hydroxyecdysone + H2O2
-
-
-
-
?
2-deoxy-20-hydroxyecdysone + O2
3-dehydro-2-deoxy-20-hydroxyecdysone + H2O2
-
-
-
?
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
probably part of the catabolic system that inactivates the molting hormones
-
-
?
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
first step in reaction sequence for the conversion of ecdysone and 20-hydroxyecdysone to their 3(alpha)-epimers
-
-
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
artificial electron acceptors in vitro in ascending order: ferricyanide, methylene blue, 2,6-dichloroindophenol, 5-methazine methyl sulfate
-
-
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
artificial electron acceptors in vitro in ascending order: ferricyanide, methylene blue, 2,6-dichloroindophenol, 5-methazine methyl sulfate
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
2,6-dichloroindophenol can act as acceptor
-
-
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
2,6-dichloroindophenol can act as acceptor
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
FAD, NAD+, NADP+, and FMN can serve as hydrogen acceptors
-
-
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
probably part of the catabolic system that inactivates the molting hormones
-
-
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
i.e. 2beta,14alpha,22,25-tetrahydroxy-5beta-cholest-7-en-3,6-dione
ir
ecdysone + O2
3-dehydroecdysone + H2O2
-
first step in reaction sequence for the conversion of ecdysone and 20-hydroxyecdysone to their 3(alpha)-epimers
-
-
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
i.e. 2beta,3beta,14alpha,22,25-pentahydroxy-5beta-cholest-7-en-6-one
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
-
-
-
-
r
ecdysone + oxidized 2,6-dichloroindophenol
3-dehydroecdysone + reduced 2,6-dichloroindophenol
-
163% activity compared to O2
-
-
r
ecdysteroids + O2
3-dehydroecdysteroids + H2O2
-
structural requirements: alpha,beta-unsaturated keto function at C-6 and several hydroxyl functions including the hydroxyls at C-3 and at C-22
-
?
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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
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
probably part of the catabolic system that inactivates the molting hormones
-
-
?
20-hydroxyecdysone + O2
3-dehydro-20-hydroxyecdysone + H2O2
-
first step in reaction sequence for the conversion of ecdysone and 20-hydroxyecdysone to their 3(alpha)-epimers
-
-
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
probably part of the catabolic system that inactivates the molting hormones
-
-
?
ecdysone + O2
3-dehydroecdysone + H2O2
-
first step in reaction sequence for the conversion of ecdysone and 20-hydroxyecdysone to their 3(alpha)-epimers
-
-
?
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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
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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
-