Reaction participants Show >> << Hide
- Name help_outline all-trans-zeaxanthin Identifier CHEBI:27547 (Beilstein: 2068416; CAS: 144-68-3) help_outline Charge 0 Formula C40H56O2 InChIKeyhelp_outline JKQXZKUSFCKOGQ-QAYBQHTQSA-N SMILEShelp_outline CC(\C=C\C=C(C)\C=C\C1=C(C)C[C@@H](O)CC1(C)C)=C/C=C/C=C(C)/C=C/C=C(C)/C=C/C1=C(C)C[C@@H](O)CC1(C)C 2D coordinates Mol file for the small molecule Search links Involved in 13 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (3R)-3-hydroxy-10'-apo-β-carotenal Identifier CHEBI:177902 Charge 0 Formula C27H36O2 InChIKeyhelp_outline HQPQTQQUHPFUOA-ZCPYHVQDSA-N SMILEShelp_outline C1C(=C(C(C[C@@H]1O)(C)C)/C=C/C(=C/C=C/C(=C/C=C/C=C(/C=C/C(=O)[H])\C)/C)/C)C 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (3R)-hydroxy-β-ionone Identifier CHEBI:53173 (Beilstein: 6504630) help_outline Charge 0 Formula C13H20O2 InChIKeyhelp_outline HFRZSVYKDDZRQY-MVIFTORASA-N SMILEShelp_outline CC(=O)\C=C\C1=C(C)C[C@@H](O)CC1(C)C 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:68104 | RHEA:68105 | RHEA:68106 | RHEA:68107 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
Publications
-
A mitochondrial enzyme degrades carotenoids and protects against oxidative stress.
Amengual J., Lobo G.P., Golczak M., Li H.N., Klimova T., Hoppel C.L., Wyss A., Palczewski K., von Lintig J.
Carotenoids are the precursors for vitamin A and are proposed to prevent oxidative damage to cells. Mammalian genomes encode a family of structurally related nonheme iron oxygenases that modify double bonds of these compounds by oxidative cleavage and cis-to-trans isomerization. The roles of the f ... >> More
Carotenoids are the precursors for vitamin A and are proposed to prevent oxidative damage to cells. Mammalian genomes encode a family of structurally related nonheme iron oxygenases that modify double bonds of these compounds by oxidative cleavage and cis-to-trans isomerization. The roles of the family members BCMO1 and RPE65 for vitamin A production and vision have been well established. Surprisingly, we found that the third family member, β,β-carotene-9',10'-oxygenase (BCDO2), is a mitochondrial carotenoid-oxygenase with broad substrate specificity. In BCDO2-deficient mice, carotenoid homeostasis was abrogated, and carotenoids accumulated in several tissues. In hepatic mitochondria, accumulated carotenoids induced key markers of mitochondrial dysfunction, such as manganese superoxide dismutase (9-fold), and reduced rates of ADP-dependent respiration by 30%. This impairment was associated with an 8-to 9-fold induction of phosphor-MAP kinase and phosphor-AKT, markers of cell signaling pathways related to oxidative stress and disease. Administration of carotenoids to human HepG2 cells depolarized mitochondrial membranes and resulted in the production of reactive oxygen species. Thus, our studies in BCDO2-deficient mice and human cell cultures indicate that carotenoids can impair respiration and induce oxidative stress. Mammalian cells thus express a mitochondrial carotenoid-oxygenase that degrades carotenoids to protect these vital organelles. << Less
FASEB J. 25:948-959(2011) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
-
Enzymatic formation of apo-carotenoids from the xanthophyll carotenoids lutein, zeaxanthin and beta-cryptoxanthin by ferret carotene-9',10'-monooxygenase.
Mein J.R., Dolnikowski G.G., Ernst H., Russell R.M., Wang X.D.
Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15'-monooxygenase (CMO1) ... >> More
Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15'-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9',10'-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC-MS and GC-MS, we identified both volatile and non-volatile apo-carotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10'-carotenal, 3-OH-β-apo-10'-carotenal, and β-apo-10'-carotenal, indicating cleavage at both the 9,10 and 9',10' carbon-carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10'-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD(+), in vitro incubation of 3-OH-β-apo-10'-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10'-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function. << Less
Arch. Biochem. Biophys. 506:109-121(2011) [PubMed] [EuropePMC]
This publication is cited by 7 other entries.
Comments
RHEA:68104 part of RHEA:26393