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Beta-carotene 15,15'-dioxygenase This is a family of bacterial and archaeal proteins that catalyzes or regulates the conversion of beta-carotene to retinal. Characterisation of BCD proteins shows them to cleave beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal. However, the oxygen atom of retinal originated not from water but from molecular oxygen, suggesting that the enzyme was a beta-carotene 15,15'-dioxygenase, rather than a mono-oxygenase that catalyzes the same biochemical reaction. |
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