BCMO1:Fe2+ cleaves betaC to atRAL

Stable Identifier
R-HSA-975635
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol, plasma membrane
Synonyms
Oxidative cleavage of beta-carotene to all-trans-retinal
ReviewStatus
5/5
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BCMO1:Fe2+ cleaves betaC to atRAL
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As long as vitamin A is needed, beta-carotene-monooxygenase (BCMO1) catalyses the cleavage of carotenes, resulting mainly in retinal (Fierce et al. 2008).
Literature References
PubMed ID Title Journal Year
18295589 In vitro and in vivo characterization of retinoid synthesis from beta-carotene

Fierce, Y, de Morais Vieira, M, Piantedosi, R, Wyss, A, Blaner, WS, Paik, J

Arch Biochem Biophys 2008
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Output
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as an event of
Catalyst Activity

beta-carotene 15,15'-dioxygenase activity of BCMO1:Fe2+ [cytosol]

Physical Entity
BCMO1:Fe2+ [cytosol] (Homo sapiens)
Activity
beta-carotene 15,15'-dioxygenase activity (GO:0003834)
Orthologous Events
BCMO1:Fe2+ cleaves betaC to atRAL (Bos taurus)
BCMO1:Fe2+ cleaves betaC to atRAL (Caenorhabditis elegans)
BCMO1:Fe2+ cleaves betaC to atRAL (Canis familiaris)
BCMO1:Fe2+ cleaves betaC to atRAL (Danio rerio)
BCMO1:Fe2+ cleaves betaC to atRAL (Drosophila melanogaster)
BCMO1:Fe2+ cleaves betaC to atRAL (Gallus gallus)
BCMO1:Fe2+ cleaves betaC to atRAL (Mus musculus)
BCMO1:Fe2+ cleaves betaC to atRAL (Rattus norvegicus)
BCMO1:Fe2+ cleaves betaC to atRAL (Sus scrofa)
BCMO1:Fe2+ cleaves betaC to atRAL (Xenopus tropicalis)
Cross References
RHEA
Authored
Stephan, R  (2010-09-19)
Reviewed
D'Eustachio, P  (2010-11-09)
Created
Jassal, B  (2010-10-01)
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