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In enzymology, β-carotene 15,15'-monooxygenase () is an enzyme that catalyzes the biological reaction :β-carotene + O2 → 2retinal This is a cleavage reaction which cleaves β-carotene, utilizes molecular oxygen, is enhanced by the presence of bile salts and thyroxine, and generates two molecules of retinal. In humans, the enzyme is present in the small intestine and liver. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The systematic name of this enzyme class is β-carotene:oxygen 15,15'-oxidoreductase (bond-cleaving). Other names in common use include β-carotene 15,15'-dioxygenase and β-carotene dioxygenase. In general, carnivores are poor converters of ionone-containing carotenoids, and pure carnivores such as cats and ferrets lack beta-carotene 15,15'-monooxygenase and cannot convert any carotenoids to retinal (resulting in none of the carotenoids being forms of vitamin A for these species). They must have preformed vitamin A in their diet. ==References== * * * 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Beta-carotene 15,15'-monooxygenase」の詳細全文を読む スポンサード リンク
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