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Supplement: Proceedings of Symposium to Honor the Memory of James Allen Olson

Carotene Oxygenases: A New Family of Double Bond Cleavage Enzymes¹

DSM Nutritional Products, Human Nutrition and Health, P.O. Box 3255, CH-4002 Basel, Switzerland

²To whom correspondence should be addressed. E-mail: Adrain.Wyss{at}dsm.com.

ß,ß-carotene 15,15'-monooxygensae (ßCMOOX) is the key enzyme involved in the metabolism of provitamin A carotenoids to retinal. Although the enzyme has been known for >40 y, it has been only within the last 2 y that the cloning and the molecular characterization of the ßCMOOX from several species was reported in literature. New clones of the carotene metabolizing enzyme have emerged, all belonging to the family of double bond cleavage enzymes, suggesting common ancestry. ßCMOOX cleaves ß,ß-carotene to retinal in an in vitro activity assay; no apo-carotenals were identified. The second enzyme involved in carotenoid metabolism, ß,ß-carotene 9',10'-dioxygenase, is responsible for the excentric cleavage pathway of carotenoids, cleaving ß,ß-carotene to 10'-apo-carotenal and ß-ionone. In an expression overview, the ßCMOOX was detected in duodenum, liver, kidney and in the lungs of chickens. In mice, the mRNA for the central cleavage enzyme was highly expressed in liver, testes, small intestine, and kidney. ßCMOOX expression was highest in epithelial and endothelial structures in both species. These results suggest that the source of vitamin A originates from carotenoids in the corresponding tissues, in addition to retinol supplied from liver stores.

KEY WORDS: • ß,ß-carotene • vitamin A • retinal • central cleavage

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