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9-cis-beta-carotene + O2
9-cis-beta-apo-10'-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
alpha-carotene + O2
beta-apo-10'-carotenal + alpha-apo-10'-carotenal
beta-carotene + O2
10'-apo-beta-carotenal + beta-ionone
-
-
-
?
beta-carotene + O2
10'-apo-carotenal + beta-ionone
beta-carotene + O2
beta-cyclocitral + beta-ionone
the enzyme is able to break the 9,10 (9',10') and 7,8 (7',8') double-bonds of beta-carotene
-
-
?
beta-cryptoxanthin + O2
3-hydroxy-beta-apo-10'-carotenal + beta-ionone
-
-
-
?
beta-cryptoxanthin + O2
3-hydroxy-beta-apo-8'-carotenal + beta-cyclocitral
-
-
-
?
beta-cryptoxanthin + O2
beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
beta-cryptoxanthin + O2
beta-apo-10'-carotenal + ?
-
main clevage product is beta-apo-10'-carotenal only small amounts of 3-OH-beta-apocarotenal are formed
-
-
?
canthaxanthin + O2
?
-
-
-
-
?
lutein + O2
3-hydroxy-alpha-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
lutein + O2
3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-alpha-ionone
-
-
-
?
lycopene + O2
6-methyl-5-hepten-2-one + ?
the enzyme also possesses oxidative cleavage activity at the 5,6 (5',6') positions of lycopene
-
-
?
zeaxanthin + O2
3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
additional information
?
-
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
alpha-carotene + O2
beta-apo-10'-carotenal + alpha-apo-10'-carotenal
-
-
-
?
alpha-carotene + O2
beta-apo-10'-carotenal + alpha-apo-10'-carotenal
-
-
-
-
?
alpha-carotene + O2
beta-apo-10'-carotenal + alpha-apo-10'-carotenal
-
-
-
-
?
beta-carotene + O2
10'-apo-carotenal + beta-ionone
-
-
-
-
?
beta-carotene + O2
10'-apo-carotenal + beta-ionone
-
-
-
-
?
beta-carotene + O2
10'-apo-carotenal + beta-ionone
-
-
-
?
beta-carotene + O2
10'-apo-carotenal + beta-ionone
-
-
-
?
lutein + O2
?
-
-
-
?
meso-zeaxanthin + O2
?
-
-
-
?
meso-zeaxanthin + O2
?
-
-
-
?
zeaxanthin + O2
3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
zeaxanthin + O2
3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
zeaxanthin + O2
3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
additional information
?
-
no substrate: lycopene, lutein, zeaxanthin, violaxanthin, or neoxanthin
-
-
?
additional information
?
-
like BCO1, EC 1.13.11.63, purified recombinant chicken BCO2 catalyzes the oxidative cleavage of the provitamin A carotenoids beta-carotene, alpha-carotene, and beta-cryptoxanthin. Its catalytic activity with beta-carotene as substrate is at least 10fold lower than that of BCO1. Purified recombinant chicken BCO2 also catalyzes the oxidative cleavage of 9-cis-beta-carotene and the non-provitamin A carotenoids zeaxanthin and lutein, and is inactive with all-trans-lycopene and beta-apo-carotenoids. Apo-10'-carotenoids are detected as enzymatic products by HPLC, and the identities are confirmed by LC-MS. Small amounts of 3-hydroxy-beta-apo-8'-carotenal are also consistently detected in BCO2-beta-cryptoxanthin reaction mixtures. With the exception of this activity with beta-cryptoxanthin, BCO2 cleaves specifically at the 9'-10'-bond to produce apo-10'-carotenoids. BCO2 is regioselective (or even regiospecific) for the trans 9'-10'-end of 9-cis-beta-carotene due to the size of the substrate tunnel. Unlike murine BCO2, chicken BCO2 cannot perform a second cleavage on beta-apo-10'-carotenal to yield rosafluene dialdehyde, and it has no activity with all-trans-lycopene, while it cleaves cis-lycopene isomers. Chicken BCO2 also does not have activity with the other beta-apocarotenals in the series (beta-apo-8'-carotenal, beta-apo-12'-carotenal, and beta-apo-14'-carotenal). Importance of the 3-hydroxy-beta-ionone ring for BCO2 cleavage, preference of BCO2 for substrates that contain a 3-hydroxy-beta-ionone ring
-
-
?
additional information
?
-
inactivity of BCO2 with xanthophylls such as zeaxanthin
-
-
?
additional information
?
-
-
inactivity of BCO2 with xanthophylls such as zeaxanthin
-
-
?
additional information
?
-
human BCO2 isoform a (human BCO2a) fails to cleave zeaxanthin, retaining the yellow color
-
-
?
additional information
?
-
-
human BCO2 isoform a (human BCO2a) fails to cleave zeaxanthin, retaining the yellow color
-
-
?
additional information
?
-
-
ScBCO2-catalyzed conversion of beta-carotene to beta-apo-10'-carotenal is followed by HPLC and LC-MS
-
-
?
additional information
?
-
-
enzyme ScBCO2 only exhibits cleavage activity towards carotenoid substrates containing two beta-ionone rings and its catalytic efficiency (kcat/Km) follows the descending order beta-carotene, alpha-carotene, lutein
-
-
?
additional information
?
-
-
ScBCO2-catalyzed conversion of beta-carotene to beta-apo-10'-carotenal is followed by HPLC and LC-MS
-
-
?
additional information
?
-
-
enzyme ScBCO2 only exhibits cleavage activity towards carotenoid substrates containing two beta-ionone rings and its catalytic efficiency (kcat/Km) follows the descending order beta-carotene, alpha-carotene, lutein
-
-
?
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all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
alpha-carotene + O2
beta-apo-10'-carotenal + alpha-apo-10'-carotenal
zeaxanthin + O2
3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
additional information
?
-
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
all-trans-beta-carotene + O2
all-trans-10'-apo-beta-carotenal + beta-ionone
-
-
-
-
?
alpha-carotene + O2
beta-apo-10'-carotenal + alpha-apo-10'-carotenal
-
-
-
-
?
alpha-carotene + O2
beta-apo-10'-carotenal + alpha-apo-10'-carotenal
-
-
-
-
?
lutein + O2
?
-
-
-
?
meso-zeaxanthin + O2
?
-
-
-
?
meso-zeaxanthin + O2
?
-
-
-
?
zeaxanthin + O2
3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
zeaxanthin + O2
3-hydroxy-beta-apo-10'-carotenal + 3-hydroxy-beta-ionone
-
-
-
?
additional information
?
-
inactivity of BCO2 with xanthophylls such as zeaxanthin
-
-
?
additional information
?
-
-
inactivity of BCO2 with xanthophylls such as zeaxanthin
-
-
?
additional information
?
-
-
ScBCO2-catalyzed conversion of beta-carotene to beta-apo-10'-carotenal is followed by HPLC and LC-MS
-
-
?
additional information
?
-
-
ScBCO2-catalyzed conversion of beta-carotene to beta-apo-10'-carotenal is followed by HPLC and LC-MS
-
-
?
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evolution
the enzyme BCO2 is a member of the polyene oxygenase gene family. The major difference between human BCO2a enzyme and mouse BCO2 is the presence of 4 aa residues, GKAA, in human BCO2, suggesting the loss of an alternate splice site in the human gene. GKAA represents an extension of human BCO2 exon 3 caused by use of an alternate donor splice site. There has been considerable genetic drift since primate BCO2 first acquired the GKAA insertion and lost its xanthophyll cleavage function
evolution
the enzyme BCO2 is a member of the polyene oxygenase gene family. The major difference between human BCO2a enzyme and mouse BCO2 is the presence of 4 aa residues, GKAA, in human BCO2, suggesting the loss of an alternate splice site in the human gene. There has been considerable genetic drift since primate BCO2 first acquired the GKAA insertion and lost its xanthophyll cleavage function
evolution
-
the enzyme BCO2 is a member of the polyene oxygenase gene family. The major difference between human BCO2a enzyme and mouse BCO2 is the presence of 4 aa residues, GKAA, in human BCO2, suggesting the loss of an alternate splice site in the human gene. There has been considerable genetic drift since primate BCO2 first acquired the GKAA insertion and lost its xanthophyll cleavage function
-
malfunction
-
knockdown of Bcdo2 by siRNA treatment in T47D cells enhances reactive oxygen species production upon carotenoid treatment. Bcdo2 siRNA-treated T47D cells show initiation of apoptosis evidenced by caspase 3 and PARP1 cleavage as established by immunoblot analyses
malfunction
-
targeted knockdown of BCDO2 results in anemia at larval stages. Marker gene analysis and staining for hemoglobin revealed that erythropoiesis is not impaired but that erythrocytes undergo apoptosis in BCDO2- deficient larvae
malfunction
-
using BCO2 knock out mice it is shown that BCO2 catalyzes beta-apocarotenoid production in vivo. Bco2-/- mice show a significant hepatic accumulation of beta-cryptoxanthin as compared to Bco1-/- and wild-type mice
malfunction
-
using transgenic LjCCD7-silenced plants an overall characterization of its role in the regulation of plant architecture, reproductive development senescence, and root symbiosis is reported. The results also link CCD7 expression with the regulation of determinate nodulation, reproduction, and senescence in Lotus japonicus
malfunction
BCO2 knockout mice, unlike wild-type mice, accumulate zeaxanthin in their retinas
malfunction
epigenetic loss of BCO2 expression is associated with prostate cancer progression, molecular mechanisms of BCO2 actions in prostate cancer, overview
malfunction
systemic depletion of BCO2 causes increased food intake and impaired hepatic lipid metabolism in mice. Compared to wild-type, BCO2 knockout mice exhibit widespread disruptions in metabolism and metabolite homeostasis, an increase in fasting blood glucose, a decrease in circulating glucagon and leptin, an elevation of plasma interleukin 1 beta and tumor necrosis factor alpha, and impaired AMP activated protein kinase signaling. The global hypothalamic metabolomic results reveal that depletion of BCO2 results in striking metabolic changes, including suppression of long-chain fatty acids transport into mitochondria, inhibition of the metabolism of dipeptides and sulfur-containing amino acids, and stimulation of local oxidative stress and inflammation in the hypothalamus of BCO2 knockout mice. Complex interplay between the hormone signaling and impaired lipid and glucose metabolism seems to account for initiation of oxidative stress, inflammation and eventual metabolic disorders in BCO2 knockout mice. Phenotype, overview
malfunction
enzyme loss induces mitochondrial hyperactivation, mitochondrial stress and changes of the mitochondrial proteome, leading to mitochondrial energy insufficiency
malfunction
-
BCO2 knockout mice, unlike wild-type mice, accumulate zeaxanthin in their retinas
-
metabolism
the enzyme is imortant in lycopene metabolism
metabolism
the substrates that are inactive with BCO2 (all-trans-lycopene and beta-apocarotenals) are substrates for BCO1
physiological function
a nonsense mutation c.196C>T in the beta-carotene oxygenase 2 gene is found to strongly associate with the yellow fat phenotype in sheep. The existence of individuals lacking this mutation, but still demonstrating yellow fat, suggests that additional mutations may cause a similar phenotype in this population. Animals homozygous for the mutation are not reported to suffer from any negative health or development traits, pointing towards a minor role of BCO2 in vitamin A formation
physiological function
coexpression of the enzyme, CCD7, and all-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase CCD8, EC 1.13.11.70, in Escherichia coli results in production of 13-apo-beta-carotenone. The sequential cleavages of beta-carotene by CCD7 and CCD8 are likely the initial steps in the synthesis of a carotenoid-derived signaling molecule that is necessary for the regulation lateral branching
physiological function
in enzyme-deficient mice, carotenoid homeostasis is abrogated, and carotenoids accumulate in several tissues. In hepatic mitochondria, accumulated carotenoids induce key markers of mitochondrial dysfunction, such as manganese superoxide dismutase, 9fold, and reduce rates of ADP-dependent respiration by 30%. This impairment is associated with an 8- to 9fold induction of phosphor-MAP kinase and phosphor-AKT, markers of cell signaling pathways related to oxidative stress and disease
physiological function
loss-of-function mutants exhibit a significant decrease in petiole length and are highly branched. The axillary buds, which are typically delayed in growth in wild-type plants, grow out to produce leaves and inflorescences. The mutant plant have smaller rosette diameters due to a decrease in the lengths of petioles and leaf blades compared with wild-type plants. The phenotypes contribute to the bushy appearance of the mutants. The double mutant, additionally lacking 10'-apo-beta-carotenal 13,14-cleaving dioxygenase activity, EC 1.13.11.70, is phenotypically indistinguishable from either single mutant, indicating an interaction consistent with both genes functioning in the same pathway. Both classes of plants show a slight increase in inflorescence number compared with wild type
physiological function
-
BCDO2 dictates apoptotic responses to carotenoids and synthetic retinoids in human cancer cells
physiological function
BCO2 catalyzes eccentric cleavage of both provitamin and non-provitamin A carotenoids which results in the formation of apo-carotenoids such as beta-apo-10' carotenal and beta-ionone
physiological function
beta-carotene 9',10'-oxygenase (BCO2) catalyzes the oxidative cleavage of carotenoids at the 9'-10'-bond to yield an ionone and an apo-10'-carotenoid
physiological function
beta-carotene 9',10'-oxygenase (BCO2) catalyzes the oxidative cleavage of carotenoids at the 9'-10'-bond to yield an ionone and an apo-10'-carotenoid. Chicken BCO2 has broader substrate specificity than BCO1, consistent with its proposed function of preventing oxidative stress brought about by carotenoid accumulation in the mitochondria. It cleaves only full-length carotenoids with ionone rings, and the hydroxylated carotenoids are cleaved to a greater extent than their hydrocarbon counterparts under the conditions tested
physiological function
in contrast to the human enzyme, mouse BCO2 is an active zeaxanthin cleavage enzyme. The binding affinities between human BCO2 and lutein, zeaxanthin, and meso-zeaxanthin are 10 to 40fold weaker than those for mouse BCO2, implying that ineffective capture of carotenoids by human BCO2 prevents cleavage of xanthophyll carotenoids
physiological function
mitochondrial beta-carotene-9',10'-oxygenase modulates prostate cancer growth via NF-kappaB inhibition in a lycopene-independent manner. Restoring bco2 expression in prostate cancer cells inhibits cell proliferation and colony formation, irrespective of lycopene exposure. Exogenous expression of either wild-type BCO2 or a mutant (enzymatically inactive) BCO2 in prostate cancer cells reduces NF-kappaB activity and decreases NF-kappaB nuclear translocation and DNA binding. BCO2 has functions that are independent of its enzymatic role in lycopene metabolism. BCO2 is a tumor suppressor in prostate cancer. BCO2-mediated inhibition of NF-kappaB signaling implies BCO2 status is important in prostate cancer progression
physiological function
the enzyme catalyzes the asymmetric cleavage of carotenoids. Enzyme BCO2 exerts its role in hypothalamic nutrient metabolism and feeding behavior. BCO2 regulates hypothalamic mitochondrial function, nutrient metabolism, and local oxidative stress and inflammation
physiological function
-
the enzyme converts beta-carotene to beta-apo-10'-carotenal, which is a precursor of the plant hormone strigolactone
physiological function
The major xanthophyll cleavage enzyme beta,beta-carotene-9',10'-dioxygenase (BCO2) is inactive in human retinas, explaining the unique accumulation of lutein, zeaxanthin, and meso-zeaxanthin in primate macula. In contrast to the murine enzyme, human BCO2 is not an active zeaxanthin cleavage enzyme. The binding affinities between human BCO2 and lutein, zeaxanthin, and meso-zeaxanthin are 10 to 40fold weaker than those for mouse BCO2, implying that ineffective capture of carotenoids by human BCO2 prevents cleavage of xanthophyll carotenoids. Primates uniquely concentrate xanthophyll carotenoids at high levels in retinal tissue
physiological function
the enzyme is critical for proper hepatic mitochondrial function
physiological function
-
the enzyme converts beta-carotene to beta-apo-10'-carotenal, which is a precursor of the plant hormone strigolactone
-
physiological function
-
in contrast to the human enzyme, mouse BCO2 is an active zeaxanthin cleavage enzyme. The binding affinities between human BCO2 and lutein, zeaxanthin, and meso-zeaxanthin are 10 to 40fold weaker than those for mouse BCO2, implying that ineffective capture of carotenoids by human BCO2 prevents cleavage of xanthophyll carotenoids
-
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Vage, D.I.; Boman, I.A.
A nonsense mutation in the beta-carotene oxygenase 2 (BCO2) gene is tightly associated with accumulation of carotenoids in adipose tissue in sheep (Ovis aries)
BMC Genet.
11
10
2010
Ovis aries (C1L3B1)
brenda
Kim, Y.; Yeom, S.; Oh, D.
Production of beta-apo-10'-carotenal from beta-carotene by human beta-carotene-9',10'-oxygenase expressed in E. coli
Biotechnol. Lett.
33
1195-1200
2011
Homo sapiens (Q9BYV7)
brenda
Amengual, J.; Lobo, G.; Golczak, M.; Li, H.; Klimova, T.; Hoppel, C.; Wyss, A.; Palczewski, K.; Von Lintig, J.
A mitochondrial enzyme degrades Carotenoids and protects against oxidative stress
FASEB J.
25
948-959
2011
Mus musculus (Q99NF1)
brenda
Kiefer, C.; Hessel, S.; Lampert, J.; Vogt, K.; Lederer, M.; Breithaupt, D.; Von Lintig, J.
Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A
J. Biol. Chem.
276
14110-14116
2001
Mus musculus (Q99NF1), Homo sapiens (Q9BYV7)
brenda
Schwartz, S.H.; Qin, X.; Loewen, M.C.
The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching
J. Biol. Chem.
279
46940-46945
2004
Arabidopsis thaliana (Q7XJM2)
brenda
Lindqvist, A.; He, Y.G.; Andersson, S.
Cell type-specific expression of beta-carotene 9',10'-monooxygenase in human tissues
J. Histochem. Cytochem.
53
1403-1412
2005
Homo sapiens (Q9BYV7)
brenda
Ledger, S.E.; Janssen, B.J.; Karunairetnam, S.; Wang, T.; Snowden, K.C.
Modified CAROTENOID CLEAVAGE DIOXYGENASE8 expression correlates with altered branching in kiwifruit (Actinidia chinensis)
New Phytol.
188
803-813
2010
Actinidia chinensis (E3T3A3)
brenda
Auldridge, M.E.; Block, A.; Vogel, J.T.; Dabney-Smith, C.; Mila, I.; Bouzayen, M.; Magallanes-Lundback, M.; DellaPenna, D.; McCarty, D.R.; Klee, H.J.
Characterization of three members of the Arabidopsis carotenoid cleavage dioxygenase family demonstrates the divergent roles of this multifunctional enzyme family
Plant J.
45
982-993
2006
Arabidopsis thaliana (Q7XJM2)
brenda
Lobo, G.P.; Isken, A.; Hoff, S.; Babino, D.; von Lintig, J.
BCDO2 acts as a carotenoid scavenger and gatekeeper for the mitochondrial apoptotic pathway
Development
139
2966-2977
2012
Danio rerio, Homo sapiens
brenda
Amengual, J.; Widjaja-Adhi, M.A.; Rodriguez-Santiago, S.; Hessel, S.; Golczak, M.; Palczewski, K.; von Lintig, J.
Two carotenoid-oxygenases contribute to mammalian pro-vitamin A metabolism
J. Biol. Chem.
288
34081-34096
2013
Mus musculus
brenda
Liu, J.; Novero, M.; Charnikhova, T.; Ferrandino, A.; Schubert, A.; Ruyter-Spira, C.; Bonfante, P.; Lovisolo, C.; Bouwmeester, H.J.; Cardinale, F.
Carotenoid cleavage dioxygenase 7 modulates plant growth, reproduction, senescence, and determinate nodulation in the model legume Lotus japonicus
J. Exp. Bot.
64
1967-1981
2013
Lotus japonicus
brenda
Amengual, J.; Gouranton, E.; van Helden, Y.G.; Hessel, S.; Ribot, J.; Kramer, E.; Kiec-Wilk, B.; Razny, U.; Lietz, G.; Wyss, A.; Dembinska-Kiec, A.; Palou, A.; Keijer, J.; Landrier, J.F.; Bonet, M.L.; von Lintig, J.
Beta-carotene reduces body adiposity of mice via BCMO1
PLoS ONE
6
e20644
2011
Mus musculus
brenda
Kim, Y.K.; Zuccaro, M.V.; Costabile, B.K.; Rodas, R.; Quadro, L.
Tissue- and sex-specific effects of beta-carotene 15,15' oxygenase (BCO1) on retinoid and lipid metabolism in adult and developing mice
Arch. Biochem. Biophys.
572
11-18
2015
Mus musculus (Q99NF1), Mus musculus C57BL/6 (Q99NF1)
brenda
Raghuvanshi, S.; Reed, V.; Blaner, W.S.; Harrison, E.H.
Cellular localization of ?-carotene 15,15 oxygenase-1 (BCO1) and beta-carotene 9,10 oxygenase-2 (BCO2) in rat liver and intestine
Arch. Biochem. Biophys.
572
19-27
2015
Rattus norvegicus (A3KN98)
brenda
Wei, T.; Jia, B.; Huang, S.; Yang, K.; Jia, C.; Mao, D.
Purification and characterization of a novel beta-carotene-9',10'-oxygenase from Saccharomyces cerevisiae ULI3
Biotechnol. Lett.
37
1993-1998
2015
Saccharomyces cerevisiae, Saccharomyces cerevisiae ULI3
brenda
Jlali, M.; Graulet, B.; Chauveau-Duriot, B.; Godet, E.; Praud, C.; Nunes, C.S.; Le Bihan-Duval, E.; Berri, C.; Duclos, M.J.
Nutrigenetics of carotenoid metabolism in the chicken a polymorphism at the beta,beta-carotene 15,15'-mono-oxygenase 1 (BCMO1) locus affects the response to dietary beta-carotene
Br. J. Nutr.
111
2079-2088
2014
Gallus gallus
brenda
Dela Sena, C.; Sun, J.; Narayanasamy, S.; Riedl, K.M.; Yuan, Y.; Curley, R.W.; Schwartz, S.J.; Harrison, E.H.
Substrate specificity of purified recombinant chicken beta-carotene 9',10'-oxygenase (BCO2)
J. Biol. Chem.
291
14609-14619
2016
Homo sapiens (B2RCV8), Gallus gallus (E1C8E0)
brenda
Guo, X.; Wu, L.; Lyu, Y.; Chowanadisai, W.; Clarke, S.L.; Lucas, E.A.; Smith, B.J.; He, H.; Wang, W.; Medeiros, D.M.; Lin, D.
Ablation of beta,beta-carotene-9,10-oxygenase 2 remodels the hypothalamic metabolome leading to metabolic disorders in mice
J. Nutr. Biochem.
46
74-82
2017
Mus musculus (Q99NF1)
brenda
Gong, X.; Marisiddaiah, R.; Zaripheh, S.; Wiener, D.; Rubin, L.P.
Mitochondrial beta-carotene 9',10' oxygenase modulates prostate cancer growth via NF-kappaB inhibition a lycopene-independent function
Mol. Cancer Res.
14
966-975
2016
Homo sapiens (Q9BYV7)
brenda
Li, B.; Vachali, P.P.; Gorusupudi, A.; Shen, Z.; Sharifzadeh, H.; Besch, B.M.; Nelson, K.; Horvath, M.M.; Frederick, J.M.; Baehr, W.; Bernstein, P.S.
Inactivity of human beta,beta-carotene-9',10'-dioxygenase (BCO2) underlies retinal accumulation of the human macular carotenoid pigment
Proc. Natl. Acad. Sci. USA
111
10173-10178
2014
Mus musculus (Q99NF1), Mus musculus, Homo sapiens (Q9BYV7), Homo sapiens, Mus musculus C57/BL6 (Q99NF1)
brenda
Meng, N.; Yan, G.L.; Zhang, D.; Li, X.Y.; Duan, C.Q.; Pan, Q.H.
Characterization of two Vitis vinifera carotenoid cleavage dioxygenases by heterologous expression in Saccharomyces cerevisiae
Mol. Biol. Rep.
46
6311-6323
2019
Vitis vinifera (U3M7F6), Vitis vinifera (U3M7R9)
brenda
Wu, L.; Guo, X.; Hartson, S.D.; Davis, M.A.; He, H.; Medeiros, D.M.; Wang, W.; Clarke, S.L.; Lucas, E.A.; Smith, B.J.; von Lintig, J.; Lin, D.
Lack of beta, beta-carotene-9',10'-oxygenase 2 leads to hepatic mitochondrial dysfunction and cellular oxidative stress in mice
Mol. Nutr. Food Res.
61
10
2017
Mus musculus (Q99NF1)
brenda