The Reaction Mechanism of the Enzyme-Catalyzed Central Cleavage of β-Carotene to Retinal
Seeing things as they really are: The enzyme catalyzing the central cleavage of β‐carotene (1) to retinal (2) is not, as previously thought, a dioxygenase. Incubation of the substrate analogue α‐carotene in the presence of highly enriched 17O2 and H218O revealed a monooxygenase mechanism.
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Veröffentlicht in: | Angewandte Chemie International Edition 2001-07, Vol.40 (14), p.2613-2617 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Seeing things as they really are: The enzyme catalyzing the central cleavage of β‐carotene (1) to retinal (2) is not, as previously thought, a dioxygenase. Incubation of the substrate analogue α‐carotene in the presence of highly enriched 17O2 and H218O revealed a monooxygenase mechanism. |
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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/1521-3773(20010716)40:14<2613::AID-ANIE2613>3.0.CO;2-Z |