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Information on EC 1.14.99.22 - ecdysone 20-monooxygenase and Organism(s) Drosophila melanogaster and UniProt Accession Q9VUF8

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IUBMB Comments
An enzyme from insect fat body or malpighian tubules involving a heme-thiolate protein (P-450). NADPH can act as ultimate hydrogen donor.
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This record set is specific for:
Drosophila melanogaster
UNIPROT: Q9VUF8
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
Synonyms
ecdysone 20-monooxygenase, cyp314a1, ecdysone 20-hydroxylase, e20mo, e-20-m, e20ohase, alpha-ecdysone c-20 hydroxylase, e20-m, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-ecdysone C-20 hydroxylase
-
-
-
-
ecdysone 20-hydroxylase
-
-
-
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ecdysone 20-monooxygenase
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ecdysone + reduced acceptor + O2 = 20-hydroxyecdysone + acceptor + H2O
show the reaction diagram
NADPH-dependent monooxygenase containing cytochrome P-450, a heme-thiolate protein
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
reduction
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ecdysone,hydrogen-donor:oxygen oxidoreductase (20-hydroxylating)
An enzyme from insect fat body or malpighian tubules involving a heme-thiolate protein (P-450). NADPH can act as ultimate hydrogen donor.
CAS REGISTRY NUMBER
COMMENTARY hide
55071-97-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ecdysone + AH2 + O2
20-hydroxyecdysone + A + H2O
show the reaction diagram
-
-
-
?
alpha-ecdysone + NADPH + O2
20-hydroxyecdysone + NADP+ + H2O
show the reaction diagram
-
-
-
?
ecdysone + AH2 + O2
20-hydroxyecdysone + A + H2O
show the reaction diagram
-
the enzyme is responsible for the conversion of the molting hormone ecdysone to its more physiologically active metabolite, 20-hydroxyecdysone
-
-
?
ecdysone + NADPH + H+ + O2
20-hydroxyecdysone + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
ecdysone + NADPH + O2
20-hydroxyecdysone + NADP+ + H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ecdysone + AH2 + O2
20-hydroxyecdysone + A + H2O
show the reaction diagram
-
-
-
?
ecdysone + AH2 + O2
20-hydroxyecdysone + A + H2O
show the reaction diagram
-
the enzyme is responsible for the conversion of the molting hormone ecdysone to its more physiologically active metabolite, 20-hydroxyecdysone
-
-
?
ecdysone + NADPH + O2
20-hydroxyecdysone + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
a cytochrome P450-dependent hydroxylase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,9-Dideoxyforskolin
-
dose dependent inhibition
2-isopropoxy-1,4-naphthoquinone
-
synthetic compound
2-methoxy-1,4-naphthoquinone
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isolated from the leaves of Impatiens glandulifera
2-propoxy-1,4-naphthoquinone
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synthetic compound
7-O-Hemisuccinyl-7-deacetyl-forskolin
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-
forskolin
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7beta-acetoxy-8,13-epoxy-1alpha,6beta,9alpha-dihydroxylabd-14-en-11-one, adenylate cyclase activator
additional information
-
inhibition profiles
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
wandering stage third instar larvae
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CP314_DROME
540
0
61690
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in S2 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Keogh, D.P.; Mitchell, M.J.; Crooks, J.R.; Smith, S.L.
Effects of the adenylate cyclase activator forskolin and its inactive derivative 1,9-dideoxyforskolin on insect cytochrome P-450 dependent steroid hydroxylase activity
Experientia
48
39-41
1991
Drosophila melanogaster, Drosophila melanogaster Canton S, Manduca sexta
Manually annotated by BRENDA team
Petryk, A.; Warren, J.T.; Marques, G.; Jarcho, M.P.; Gilbert, L.I.; Kahler, J.; Parvy, J.P.; Li, Y.; Dauphin-Villemant, C.; O'Connor, M.B.
Shade is the Drosophila P450 enzyme that mediates the hydroxylation of ecdysone to the steroid insect molting hormone 20-hydroxyecdysone
Proc. Natl. Acad. Sci. USA
100
13773-13778
2003
Drosophila melanogaster (Q9VUF8)
Manually annotated by BRENDA team
Mitchell, M.J.; Brescia, A.I.; Smith, S.L.; Morgan, E.D.
Effects of the compounds 2-methoxynaphthoquinone, 2-propoxynaphthoquinone, and 2-isopropoxynaphthoquinone on ecdysone 20-monooxygenase activity
Arch. Insect Biochem. Physiol.
66
45-52
2007
Aedes aegypti, Drosophila melanogaster, Manduca sexta
Manually annotated by BRENDA team
Rauschenbach, I.; Gruntenko, N.; Chentsova, N.; Adonyeva, N.; Alekseev, A.
Role of ecdysone 20-monooxygenase in regulation of 20-hydroxyecdysone levels by juvenile hormone and biogenic amines in Drosophila
J. Comp. Physiol. B
178
27-32
2008
Drosophila melanogaster, Drosophila virilis
Manually annotated by BRENDA team