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Information on EC 1.14.19.21 - cholesterol 7-desaturase
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1.14.19.21 cholesterol 7-desaturaseIUBMB Comments
The enzyme, characterized from several organisms including the worm Caenorhabditis elegans, the fly Drosophila melanogaster, and the ciliate Tetrahymena thermophila, is a Rieske oxygenase. In insects it participates in the the biosythesis of ecdysteroid hormones. The electrons are transferred from NAD(P)H via an electron transfer chain likely to include ferredoxin reductase and ferredoxin. The enzyme differs from regular desaturases, such as EC 1.14.19.20, 7-sterol 5(6)-desaturase, which are cytochrome b5-dependent and contain the three His-boxes that are typical to most desaturases.
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Word Map
- 1.14.19.21
- 7-dehydrocholesterol
- steroid
- ecdysteroids
- nematodes
-
dafachronic
- tetrahymena
-
ciliate
- oxygenases
- rnai
- arthropods
-
bombyx
- thermophila
The enzyme appears in viruses and cellular organisms
Synonyms
pmnvd, des7p, cholesterol 7-desaturase, cholesterol 7,8-dehydrogenase, daf-36/neverland, rieske domain oxygenase neverland, sterol c7(8)-desaturase, c-7 cholesterol desaturase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cholesterol 7,8-dehydrogenase
DAF-36/Neverland
Des7p
Nvd
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cholesterol + O2 + NAD(P)H + H+ = cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
cholesterol,NAD(P)H:oxygen oxidoreductase (7,8 dehydrogenating)
The enzyme, characterized from several organisms including the worm Caenorhabditis elegans, the fly Drosophila melanogaster, and the ciliate Tetrahymena thermophila, is a Rieske oxygenase. In insects it participates in the the biosythesis of ecdysteroid hormones. The electrons are transferred from NAD(P)H via an electron transfer chain likely to include ferredoxin reductase and ferredoxin. The enzyme differs from regular desaturases, such as EC 1.14.19.20, 7-sterol 5(6)-desaturase, which are cytochrome b5-dependent and contain the three His-boxes that are typical to most desaturases.
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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
22-cholesten-3beta-ol + NADH + H+
7,22-cholestadiene-3beta-ol + NAD+ + H2O
-
-
-
?
22-cholesten-3beta-ol + NADPH + H+
7,22-cholestadiene-3beta-ol + NADP+ + H2O
-
-
-
?
5alpha-cholest-22-en-3beta-ol + O2 + NADH + H+
5alpha-cholesta-7,22-dien-3beta-ol + NAD+ + H2O
-
-
-
-
?
5alpha-cholest-22-en-3beta-ol + O2 + NADPH + H+
5alpha-cholesta-7,22-dien-3beta-ol + NADP+ + H2O
-
-
-
-
?
5alpha-cholestan-3beta-ol + O2 + NADH + H+
5alpha-cholest-7-en-3beta-ol + NAD+ + H2O
-
-
-
-
?
5alpha-cholestan-3beta-ol + O2 + NADPH + H+
5alpha-cholest-7-en-3beta-ol + NADP+ + H2O
-
-
-
-
?
cholesta-5,22-dien-3beta-ol + O2 + NADH + H+
cholesta-5,7,22-trien-3beta-ol + NAD+ + H2O
-
-
-
-
?
cholesta-5,22-dien-3beta-ol + O2 + NADPH + H+
cholesta-5,7,22-trien-3beta-ol + NADP+ + H2O
-
-
-
-
?
cholestan-3beta-ol + NADH + H+
7-cholesten-3beta-ol + NAD+ + H2O
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-
-
?
cholestan-3beta-ol + NADPH + H+
7-cholesten-3beta-ol + NADP+ + H2O
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-
-
?
cholestanol + O2 + NADPH + H+
cholesta-5,7,22-trien-3beta-ol + NADP+ + H2O
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main product
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?
cholesterol + O2 + NAD(P)H + H+
cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
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-
-
?
stigmastanol + O2 + NADPH + H+
5alpha-24-ethylcholest-7-en-3beta-ol + NADP+ + H2O
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-
main product
-
?
stigmasterol + O2 + NADPH + H+
(3beta,22E)-stigmasta-5,7,22-trien-3-ol + NADP+ + H2O
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-
main product
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NAD+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NAD+ + H2O
-
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NAD+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
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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
22-cholesten-3beta-ol + NADH + H+
7,22-cholestadiene-3beta-ol + NAD+ + H2O
-
-
-
?
22-cholesten-3beta-ol + NADPH + H+
7,22-cholestadiene-3beta-ol + NADP+ + H2O
-
-
-
?
5alpha-cholest-22-en-3beta-ol + O2 + NADH + H+
5alpha-cholesta-7,22-dien-3beta-ol + NAD+ + H2O
-
-
-
-
?
5alpha-cholest-22-en-3beta-ol + O2 + NADPH + H+
5alpha-cholesta-7,22-dien-3beta-ol + NADP+ + H2O
-
-
-
-
?
5alpha-cholestan-3beta-ol + O2 + NADH + H+
5alpha-cholest-7-en-3beta-ol + NAD+ + H2O
-
-
-
-
?
5alpha-cholestan-3beta-ol + O2 + NADPH + H+
5alpha-cholest-7-en-3beta-ol + NADP+ + H2O
-
-
-
-
?
cholesta-5,22-dien-3beta-ol + O2 + NADH + H+
cholesta-5,7,22-trien-3beta-ol + NAD+ + H2O
-
-
-
-
?
cholesta-5,22-dien-3beta-ol + O2 + NADPH + H+
cholesta-5,7,22-trien-3beta-ol + NADP+ + H2O
-
-
-
-
?
cholestan-3beta-ol + NADH + H+
7-cholesten-3beta-ol + NAD+ + H2O
-
-
-
?
cholestan-3beta-ol + NADPH + H+
7-cholesten-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NAD+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NAD+ + H2O
-
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NAD+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S]-center
the enzyme structure contains a Rieske [2Fe-2S] domain motif 107AxxG209 with the highly conserved sequence C-X-H-X16-17-C-X2-H and a non-heme iron-binding motif E-X3-D-X2-H-X4-H
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
the enzyme structure contains a Rieske [2Fe-2S] domain motif 107AxxG209 with the highly conserved sequence C-X-H-X16-17-C-X2-H and a non-heme iron-binding motif E-X3-D-X2-H-X4-H
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Melanoma
NVD-BM-mediated genetic biosensor triggers accumulation of 7-dehydrocholesterol and inhibits melanoma via Akt1/NF-?B signaling.
Neoplasms
NVD-BM-mediated genetic biosensor triggers accumulation of 7-dehydrocholesterol and inhibits melanoma via Akt1/NF-?B signaling.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the expression of PmNvd is dominantly in the Y-organ, but changes during molting period. The PmNvd mRNA level is low in intermolt and early premolt stages, then dramatically increases in the mid premolt stage. No enzyme expression in eyestalk, brain, thoracic ganglia, nerve cord, hepatopancreas, ovary, gills, muscle, and lymphoid organ, RT-PCR expression analysis
brenda
additional information
-
the expression of PmNvd is dominantly in the Y-organ, but changes during molting period. The PmNvd mRNA level is low in intermolt and early premolt stages, then dramatically increases in the mid premolt stage. No enzyme expression in eyestalk, brain, thoracic ganglia, nerve cord, hepatopancreas, ovary, gills, muscle, and lymphoid organ, RT-PCR expression analysis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme sequence contains the transmembrane motif 33WxxF59
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
silencing of PmNvd transcript in shrimp by specific double-stranded RNA (dsNvd) leads to prolonged molt duration with abnormal molting progression, i.e. the molting process got stuck at early premolt stage. In addition, the 20-hydroxyecdysone titer in hemolymph of dsNvd-injected shrimps is significantly reduced compared with that in NaCl-injected shrimps. Phenotype, overview
metabolism
the cholesterol 7,8-dehydrogenase catalyzes the first step of the ecdysteroid biosynthesis converting cholesterol to 7-dehydrocholesterol
physiological function
physiological function
-
the enzyme regulates DAF-12 activities for reproductive development and longevity by controlling dafachronic acids production
physiological function
function of the enzyme in the molting process and molt regulation, crucial role of PmNvd in molt progression, particularly during the initiation of premolt phase via the regulation of ecdysteroid production
Show AA Sequence and Transmembrane Helices (864 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction and expression of double-stranded RNA specific to PmNvd (dsNvd) for silencing of the enzyme, effect of PmNvd knockdown on molting duration, phenotype, overview
additional information
-
construction and expression of double-stranded RNA specific to PmNvd (dsNvd) for silencing of the enzyme, effect of PmNvd knockdown on molting duration, phenotype, overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amiino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR expression analysis
expressed in Drosophila melanogaster S2 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wollam, J.; Magomedova, L.; Magner, D.B.; Shen, Y.; Rottiers, V.; Motola, D.L.; Mangelsdorf, D.J.; Cummins, C.L.; Antebi, A.
The Rieske oxygenase DAF-36 functions as a cholesterol 7-desaturase in steroidogenic pathways governing longevity
Aging Cell
10
879-884
2011
Caenorhabditis elegans
brenda
Yoshiyama-Yanagawa, T.; Enya, S.; Shimada-Niwa, Y.; Yaguchi, S.; Haramoto, Y.; Matsuya, T.; Shiomi, K.; Sasakura, Y.; Takahashi, S.; Asashima, M.; Kataoka, H.; Niwa, R.
The conserved Rieske oxygenase DAF-36/Neverland is a novel cholesterol-metabolizing enzyme
J. Biol. Chem.
286
25756-25762
2011
Xenopus laevis (F7J184), Xenopus laevis, Ciona intestinalis (F7J186), Ciona intestinalis, Hemicentrotus pulcherrimus (F7J188), Hemicentrotus pulcherrimus, Caenorhabditis elegans (Q17938), Caenorhabditis elegans, Bombyx mori (Q1JUZ2), Bombyx mori, Danio rerio (Q6DHJ3), Danio rerio
brenda
Najle, S.R.; Nusblat, A.D.; Nudel, C.B.; Uttaro, A.D.
The sterol-C7 desaturase from the ciliate Tetrahymena thermophila is a Rieske oxygenase, which is highly conserved in animals
Mol. Biol. Evol.
30
1630-1643
2013
Tetrahymena thermophila
brenda
Poklepovich, T.; Urtasun, N.; Miranda, M.; Nusblat, A.; Nudel, C.
Expression and functional characterization of a C-7 cholesterol desaturase from Tetrahymena thermophila in an insect cell line
Steroids
96
132-139
2015
Tetrahymena thermophila (I7ML19), Tetrahymena thermophila
brenda
Sathapondecha, P.; Panyim, S.; Udomkit, A.
An essential role of Rieske domain oxygenase Neverland in the molting cycle of black tiger shrimp, Penaeus monodon
Comp. Biochem. Physiol. A
213
11-19
2017
Penaeus monodon (A0A2I4PEL8), Penaeus monodon
brenda
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Release 2023.1 (January 2023)
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