Carotene oxygenases: a new family of double bond cleavage enzymes

Abstract

Beta,beta-carotene 15,15'-monooxygensae (betaCMOOX) 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 betaCMOOX 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. BetaCMOOX cleaves beta,beta-carotene to retinal in an in vitro activity assay; no apo-carotenals were identified. The second enzyme involved in carotenoid metabolism, beta,beta-carotene 9',10'-dioxygenase, is responsible for the excentric cleavage pathway of carotenoids, cleaving beta,beta-carotene to 10'-apo-carotenal and beta-ionone. In an expression overview, the betaCMOOX 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. betaCMOOX 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.