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The Reaction Mechanism of the Enzyme‐Catalyzed Central Cleavage of β ‐Carotene to Retinal
Author(s) -
Leuenberger Michele G.,
EngelochJarret Caroline,
Woggon WolfD.
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010716)40:14<2613::aid-anie2613>3.0.co;2-z
Subject(s) - cleavage (geology) , dioxygenase , chemistry , enzyme , monooxygenase , catalysis , retinal , stereochemistry , substrate (aquarium) , substrate specificity , biochemistry , oxygenase , carotene , biology , organic chemistry , ecology , cytochrome p450 , paleontology , fracture (geology)
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 17 O 2 and H 2 18 O revealed a monooxygenase mechanism.