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
Hauptverfasser: Leuenberger, Michele G., Engeloch-Jarret, Caroline, Woggon, Wolf-D.
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.
ISSN:1433-7851
1521-3773
DOI:10.1002/1521-3773(20010716)40:14<2613::AID-ANIE2613>3.0.CO;2-Z