ArticleThe Journal of biological chemistry2015
Utilization of Dioxygen by Carotenoid Cleavage Oxygenases.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 61 citations in OpenAlex.
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- Retinoid dynamics in vision: from visual cycle biology to retina disease treatments.Pharmacology & therapeutics · 2025Review
- Spectroscopy and crystallography define carotenoid oxygenases as a new subclass of mononuclear non-heme FeThe Journal of biological chemistry · 2025Article
- A structural and functional model for alkene dioxygenases.Journal of inorganic biochemistry · 2025Article
- Engineering a coenzyme-independent dioxygenase for one-step production of vanillin from ferulic acid.Applied and environmental microbiology · 2024Article
- Rationally Guided Improvement of NOV1 Dioxygenase for the Conversion of Lignin-Derived Isoeugenol to Vanillin.Biochemistry · 2023Article
- A Computer Simulation Insight into the Formation of Apocarotenoids: Study of the Carotenoid Oxygenases BCO1 and BCO2 and Their Interaction with Putative Substrates.Molecules (Basel, Switzerland) · 2022Article
- Aster la vista: Unraveling the biochemical basis of carotenoid homeostasis in the human retina.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Article
- Retinal pigment epithelium 65 kDa protein (RPE65): An update.Progress in retinal and eye research · 2022Review
- Preparation of carotenoid cleavage dioxygenases for X-ray crystallography.Methods in enzymology · 2022Article
- Structural and Functional Analysis of Nonheme Iron Enzymes BCMO-1 and BCMO-2 fromFrontiers in molecular biosciences · 2022Article
- The Structural and Biochemical Basis of Apocarotenoid Processing by β-Carotene Oxygenase-2.ACS chemical biology · 2021Article
- Metabolism of Carotenoids in Mammals.Advances in experimental medicine and biology · 2021Article
- Molecular components affecting ocular carotenoid and retinoid homeostasis.Progress in retinal and eye research · 2021Review
- Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Carotenoid metabolism at the intestinal barrier.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Structural and mechanistic aspects of carotenoid cleavage dioxygenases (CCDs).Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Structural basis for carotenoid cleavage by an archaeal carotenoid dioxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Identification of functionally important residues and structural features in a bacterial lignostilbene dioxygenase.The Journal of biological chemistry · 2019Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Carotenoid cleavage oxygenases (CCOs) are non-heme, Fe(II)-dependent enzymes that participate in biologically important metabolic pathways involving carotenoids and apocarotenoids, including retinoids, stilbenes, and related compounds. CCOs typically catalyze the cleavage of non-aromatic double bonds by dioxygen (O2) to form aldehyde or ketone products. Expressed only in vertebrates, the RPE65 sub-group of CCOs catalyzes a non-canonical reaction consisting of concerted ester cleavage and trans-cis isomerization of all-trans-retinyl esters. It remains unclear whether the former group of CCOs functions as mono- or di-oxygenases. Additionally, a potential role for O2 in catalysis by the RPE65 group of CCOs has not been evaluated to date. Here, we investigated the pattern of oxygen incorporation into apocarotenoid products of Synechocystis apocarotenoid oxygenase. Reactions performed in the presence of (18)O-labeled water and (18)O2 revealed an unambiguous dioxygenase pattern of O2 incorporation into the reaction products. Substitution of Ala for Thr at position 136 of apocarotenoid oxygenase, a site predicted to govern the mono- versus dioxygenase tendency of CCOs, greatly reduced enzymatic activity without altering the dioxygenase labeling pattern. Reevaluation of the oxygen-labeling pattern of the resveratrol-cleaving CCO, NOV2, previously reported to be a monooxygenase, using a purified enzyme sample revealed that it too is a dioxygenase. We also demonstrated that bovine RPE65 is not dependent on O2 for its cleavage/isomerase activity. In conjunction with prior research, the results of this study resolve key issues regarding the utilization of O2 by CCOs and indicate that dioxygenase activity is a feature common among double bond-cleaving CCOs.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.