Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.19.21 - cholesterol 7-desaturase and Organism(s) Hemicentrotus pulcherrimus and UniProt Accession F7J188

for references in articles please use BRENDA:EC1.14.19.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Hemicentrotus pulcherrimus
UNIPROT: F7J188
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Hemicentrotus pulcherrimus
The enzyme appears in selected viruses and cellular organisms
Synonyms
pmnvd, des7p, cholesterol 7-desaturase, cholesterol 7,8-dehydrogenase, daf-36/neverland, sterol c7(8)-desaturase, c-7 cholesterol desaturase, rieske domain oxygenase neverland, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cholesterol 7,8-dehydrogenase
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
show the reaction diagram
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + 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
cholesterol + O2 + NADH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
show the reaction diagram
-
-
-
?
cholesterol + O2 + NADPH + H+
cholesta-5,7-dien-3beta-ol + NADP+ + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NVD_HEMPU
469
2
53055
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Drosophila melanogaster S2 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team