Enzymology of vertebrate carotenoid oxygenases.

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  • Author(s): Harrison EH;Harrison EH;Harrison EH; Kopec RE; Kopec RE; Kopec RE
  • Source:
    Biochimica et biophysica acta. Molecular and cell biology of lipids [Biochim Biophys Acta Mol Cell Biol Lipids] 2020 Nov; Vol. 1865 (11), pp. 158653. Date of Electronic Publication: 2020 Feb 05.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural; Review
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101731727 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-2618 (Electronic) Linking ISSN: 13881981 NLM ISO Abbreviation: Biochim Biophys Acta Mol Cell Biol Lipids Subsets: MEDLINE
    • Publication Information:
      Original Publication: Amsterdam : Elsevier
    • Subject Terms:
      Carotenoids/*metabolism ; Dioxygenases/*genetics ; Oxidative Stress/*genetics ; Oxygenases/*genetics ; beta-Carotene 15,15'-Monooxygenase/*genetics; Animals ; Catalysis ; Dioxygenases/chemistry ; Humans ; Mice ; Mice, Knockout ; Oxygenases/chemistry ; Vertebrates/genetics ; beta-Carotene 15,15'-Monooxygenase/chemistry
    • Abstract:
      Mammals and higher vertebrates including humans have only three members of the carotenoid cleavage dioxygenase family of enzymes. This review focuses on the two that function as carotenoid oxygenases. β-Carotene 15,15'-dioxygenase (BCO1) catalyzes the oxidative cleavage of the central 15,15' carbon-carbon double of β-carotene bond by addition of molecular oxygen. The product of the reaction is retinaldehyde (retinal or β-apo-15-carotenal). Thus, BCO1 is the enzyme responsible for the conversion of provitamin A carotenoids to vitamin A. It also cleaves the 15,15' bond of β-apocarotenals to yield retinal and of lycopene to yield apo-15-lycopenal. β-Carotene 9',10'-dioxygenase (BCO2) catalyzes the cleavage of the 9,10 and 9',10' double bonds of a wider variety of carotenoids, including both provitamin A and non-provitamin A carotenoids, as well as the xanthophylls, lutein and zeaxanthin. Indeed, the enzyme shows a marked preference for utilization of these xanthophylls and other substrates with hydroxylated terminal rings. Studies of the phenotypes of BCO1 null, BCO2 null, and BCO1/2 double knockout mice and of humans with polymorphisms in the enzymes, has clarified the role of these enzymes in whole body carotenoid and vitamin A homeostasis. These studies also demonstrate the relationship between enzyme expression and whole body lipid and energy metabolism and oxidative stress. In addition, relationships between BCO1 and BCO2 and the development or risk of metabolic diseases, eye diseases and cancer have been observed. While the precise roles of the enzymes in the pathophysiology of most of these diseases is not presently clear, these gaps in knowledge provide fertile ground for rigorous future investigations. This article is part of a Special Issue entitled Carotenoids: Recent Advances in Cell and Molecular Biology edited by Johannes von Lintig and Loredana Quadro.
      Competing Interests: Declaration of competing interest The authors declare that they have no competing or conflicting interests in the publication of this manuscript.
      (Copyright © 2020 Elsevier B.V. All rights reserved.)
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    • Grant Information:
      R01 DK044498 United States DK NIDDK NIH HHS; R01 DK101251 United States DK NIDDK NIH HHS; R01 HL049879 United States HL NHLBI NIH HHS
    • Contributed Indexing:
      Keywords: Beta-carotene; Carotenoid oxygenases; Dioxygenase; Vitamin A; Xanthophylls
    • Accession Number:
      36-88-4 (Carotenoids)
      EC 1.13.- (Oxygenases)
      EC 1.13.- (carotenoid oxygenase)
      EC 1.13.11.- (Dioxygenases)
      EC 1.14.99.- (BCO2 protein, human)
      EC 1.14.99.36 (BCO1 protein, human)
      EC 1.14.99.36 (beta-Carotene 15,15'-Monooxygenase)
    • Publication Date:
      Date Created: 20200209 Date Completed: 20201231 Latest Revision: 20231119
    • Publication Date:
      20231215
    • Accession Number:
      PMC10655466
    • Accession Number:
      10.1016/j.bbalip.2020.158653
    • Accession Number:
      32035229