β-carotene-15,15'-monooxygenase

Β-carotene-15,15′-monooxygenase
Properties of human protein
Mass / length primary structure	547 amino acids
Cofactor	iron
Identifier
Gene name	BCMO1
External IDs	OMIM : 605748 ; UniProt : Q9HAY6 ;
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

Oxidative degradation of β-carotene (top) under the action of 15,15′-dioxygenase leads to two equivalents of all- trans -retinal (bottom) via a dioxetane (middle ).

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.)

[1] UniProt Q9HAY6

[Gossauer-2] Albert Gossauer: Structure and reactivity of biomolecules , Verlag Helvetica Chimica Acta, Zurich, 2006, pp. 147-148, ISBN 978-3-906390-29-1 .