β-carotene-15,15'-monooxygenase
Β-carotene-15,15′-monooxygenase | ||
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Properties of human protein | ||
Mass / length primary structure | 547 amino acids | |
Cofactor | iron | |
Identifier | ||
Gene name | BCMO1 | |
External IDs | ||
Enzyme classification | ||
EC, category | 1.14.99.36 , monooxygenase | |
Response type | Oxidative cleavage | |
Substrate | β-carotene + O 2 | |
Products | Retinal | |
Occurrence | ||
Homology family | Carotenoid oxygenase | |
Parent taxon | Bacteria, animals |
Beta-carotene – 15,15′-monooxygenase (BCO) is the enzyme that breaks down β-carotene into two retinal molecules and thus activates it as vitamin A. In humans, this process takes place primarily in the intestines , but also in epithelial cells of the retina , liver and kidneys . Rare mutations in the human BCMO - gene can be inherited Hypercarotinämie lead with vitamin A deficiency.
BCO is one of the carotenoid oxygenases and has evolved with multicellular animals . Homologous proteins are present in a few types of bacteria.
Catalyzed reaction
Individual evidence
- ↑ UniProt Q9HAY6
- ^ Albert Gossauer: Structure and reactivity of biomolecules , Verlag Helvetica Chimica Acta, Zurich, 2006, pp. 147-148, ISBN 978-3-906390-29-1 .
Web links
Wikibooks: Biochemistry and Pathobiochemistry: Retinol Metabolism - Learning and Teaching Materials
- Jennifer McDowall / Interpro: Protein Of The Month: Carotenoid Oxygenase. (engl.)