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Information on EC 1.14.99.36 - beta-carotene 15,15'-monooxygenase
for references in articles please use BRENDA:EC1.14.99.36
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Old data from external sources may still be available.
Please check here for current data: EC 1.13.11.63
Please check here for current data: EC 1.13.11.63
deleted. Now classified as EC 1.13.11.63, beta-carotene 15,15'-dioxygenase
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.99 Miscellaneous
1.14.99.36 beta-carotene 15,15'-monooxygenase
IUBMB Comments
Requires bile salts and Fe(II). This animal enzyme catalyses the reaction in three stages, epoxidation of the 15,15′-double bond, hydration of the epoxide leading to ring opening, and oxidative cleavage of the diol formed. Thus only one atom of the dioxygen is incorporated into each retinal molecule. The nature of the acceptor listed in reactions (1a) and (1c) is assumed to be iron within the active site. Formerly classified in EC 1.13.11 as it had been thought to be a dioxygenase. cf. EC 1.13.11.63, β-carotene 15,15′-dioxygenase.
Synonyms
beta-carotene 15,15'-dioxygenase, more
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DISEASE 
TITLE OF PUBLICATION
LINK TO PUBMED
Diabetes Mellitus
Beta-carotene 15,15'-dioxygenase activity in streptozotocin-induced diabetic rats.
Vitamin A Deficiency
Carotene dioxygenase (EC 1.13.11.21) activity in rat intestine: effects of vitamin A deficiency and of pregnancy.
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.1016
beta-carotene
-
recombinant His6-tagged enzyme, pH and temperature not specified in the publication
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
BCMO1 is a member of an evolutionary well-conserved family of carotenoid cleavage oxygenases
evolution
-
BCMO1 is a member of an evolutionary well-conserved family of carotenoid cleavage oxygenases
evolution
Mus musculus C57/BL6 / 129 Sv
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BCMO1 is a member of an evolutionary well-conserved family of carotenoid cleavage oxygenases
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malfunction
-
a nonsense mutation c.196C-T in the beta-carotene oxygenase 2 BCO2 gene is strongly associated with the yellow fat phenotype in sheep that is caused by accumulation of carotenoids in adipose tissue, a recessive trait. But animals homozygous for the mutation do not suffer from any negative health or development traits, pointing towards a minor role of BCO2 in vitamin A formation
malfunction
-
BCMO1 knock-out mice become vitamin A deficient despite expressing BCDO2. Hepatic BCDO2 expression is significantly elevated in BCMO1 KO mice compared with wild-type mice, leading to a significant increase in beta-apo-12'-carotenal or beta-apo-10'-carotenal concentration. BCMO1 KO mice reveal a large accumulation of beta-carotene in tissues (liver, lung, adipose tissue) of animals on a beta-carotene-enriched diet. Increased susceptibility of BCMO1 KO mice to diet induced obesity, coupled with increased expression of PPAR-gamma-induced genes. Knockout of BCMO1 alters serum lipid levels and leads to the development of liver steatosis in mice
malfunction
-
Bcmo1-/- mice show increased expression of Bcdo2 in adipocytes and beta-10'-apocarotenol accumulates as the major beta-carotene derivative. Bcmo1-/- mice have a lower average body weight than wild-type mice
malfunction
-
reduced BCMO1 expression in normal preneoplastic intestine of folate-deficient tumor-prone mice. A mouse model develops intestinal tumors after low dietary folate
malfunction
-
transfection of cells with BCMO1 siRNA inhibits BCMO1 expression, enhances cancer migration and invasion, and increases expression of MMP7 and MMP28
malfunction
-
lack of CMOI in the developing tissues further exacerbates the severity of vitamin A deficiency and thus the embryonic malformations of retinol-binding protein-deficient mice, phenotypes, overview
malfunction
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genetic disruption of BCO1 results in beta-carotene accumulation and vitamin A deficiency accompanied by a BCO2-dependent production of minor amounts of beta-apo-10'-carotenol, which can be esterified and transported by the same proteins as vitamin A but with a lower affinity and slower reaction kinetics. all-trans-Retinol treatment of vitamin A-deprived Bco1-/- mice decreases hepatic retinol-binding protein levels
metabolism
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carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
metabolism
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carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
metabolism
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Bcmo1 and retinal dehydrogenase 1 are key enzymes in the retinoid metabolism of inguinal white adipose tissue
metabolism
-
carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
metabolism
-
carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
metabolism
-
carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
metabolism
-
carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
metabolism
-
carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
metabolism
-
carotenoids and apo-carotenoids are converted to retinal by beta-carotene 15,15'-dioxygenase, BCDO, by beta-carotene 15,15'-monooxygenase, BCMO, and by apo-carotenoid 15,15'-oxygenase, ACO, EC 1.14.99.41
metabolism
-
beta-carotene 15,15'-monooxygenase is a key enzyme in vitamin A metabolism
physiological function
-
enzyme deletion mutants show a significant increase in the total carotenoid content
physiological function
-
beta-carotene cleavage oxygenase determines the beta-carotene content of the cell. Deletion of the cco1 gene, does not affect growth, morphology or pathogenicity
physiological function
-
larvae of ninaB mutants show no photophobic behavior indicating that NinaB is essential for larval light perception. ninaB mutant flies exhibit impaired chromophore production and consequently lack visual pigments. Visual pigment production essentially depends on NinaB
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development. Model of the putative mechanism for the regulation of BCMO1 by dietary fat and PPARgamma, overview
physiological function
-
beta,beta-carotene 15,15'-monooxygenase-1, BCMO1, is a key enzyme in vitamin A metabolism in mammals. BCMO1 plays a significant physiological role in the local regulation of vitamin A and retinal in reproduction and development
physiological function
-
quantitatively important role for BCO2 in carotenoid degradation, which might indicate a broad enzyme specificity for carotenoids
physiological function
-
increased intestinal enzyme expression occurs in obesity and dyslipedemia and may affect the plasma retinol status, overview
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
carotenoid 15,15'-oxygenases produce retinal from carotenoids
physiological function
-
BCMO1 catalyzes the symmetric cleavage of carotenoids. BCMO1 is implicated as a regulator of lipid metabolism. BCMO1 exerts an additional function on retinoid metabolism by influencing retinyl ester formation via modulation of lecithin:retinol acyltransferase activity, thus confirming the critical role of BCMO1 for embryonic retinoid metabolism
physiological function
-
BCMO1 catalyzes the symmetric cleavage of carotenoids. BCMO1 is the key enzyme for beta-carotene conversion into vitamin A. BCMO1-dependent decrease in PPAR-gamma target gene expression is observed during beta-carotene supplementation in inguinal white adipose tissue. The intestine-specific transcription factor intestine-specific homeobox in mouse intestine is an important regulator of BCMO1 expression. Activation of intestine-specific homeobox results in repression of SR-BI and BCMO1 expression thereby controlling beta-carotene absorption as well as vitamin A production
physiological function
-
BCMO1 catalyzes the symmetric cleavage of carotenoids
physiological function
-
BCMO1 catalyzes the symmetric cleavage of carotenoids
physiological function
-
BCMO1 catalyzes the symmetric cleavage of carotenoids
physiological function
-
BCMO1 catalyzes the symmetric cleavage of carotenoids
physiological function
-
beta-carotene plays an important role in the control of body adiposity in mice. The enzyme is a critical molecular player for the regulation of peroxisome proliferator-activated receptor gamma activity in adipocytes
physiological function
-
beta,beta-carotene 15,15'-monooxygenase and its substrate beta-carotene modulate migration and invasion in colorectal carcinoma cells. Increased beta-carotene consumption is linked to antitumor effects. Retinoic acid reduces the invasiveness in cancer, through inhibition of matrix metalloproteinases
physiological function
-
beta,beta-carotene 15,15'-monooxygenase and its substrate beta-carotene modulate migration and invasion in colorectal carcinoma cells. Increased beta-carotene consumption is linked to antitumor effects. Retinoic acid reduces the migration and invasiveness in cancer, through inhibition of matrix metalloproteinase MMP28 expression, 5-aza-2'-deoxycytidine reduces LoVo cell invasiveness
physiological function
-
cmo1 gene transcription may be subject to negative feedback by accumulation of its metabolic products in intestine and liver. Non-gastrointestinal CMO1 may be required for tissue-specific conversion of beta-carotene into vitamin A
physiological function
-
CMOI is expressed in embryonic tissues, suggesting that beta-carotene provides retinoids locally during development. CMOI exerts an additional function on retinoid metabolism by influencing retinyl ester formation via modulation of lecithin:retinol acyltransferase activity, at least in developing tissues
physiological function
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beta-carotene 15,15'-oxygenase (BCO1) produces vitamin A from carotenoids in food. BCO1 catalyzes the oxidative cleavage of the 15-15'-double bond of major dietary provitamin A carotenoids,beta-apocarotenals, and lycopene
physiological function
-
beta-carotene-15,15'-oxygenase BCO1, but not beta-carotene-9',10'-oxygenase BCO2, is critical for retinoid homeostasis. In wild-type mice, beta-apo-10'-carotenol is converted to retinoids by BCO1
physiological function
Mus musculus C57/BL6 / 129 Sv
-
BCMO1 is the major enzyme for vitamin A production
-
additional information
-
beta-carotene represses Ppar gamma and CCAAT/enhancer-binding protein alpha expression in mature adipocytes
additional information
-
dietary beta-carotene downregulates peroxisome proliferator-activated receptor gamma and peroxisome proliferator-activated receptor gamma target genes in adipose tissue of wild-type mice. Supplementation of beta-carotene alters gene expression profiles in wild-type but not in Bcmo1-/- mice
additional information
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beta-carotene treatment antagonizes peroxisome proliferator-activated receptor gamma activity in HEK-293 cells that stably express CMO1 wild-type, but not in cells that express the CMO1 mutant or vector alone having implications for local vitamin A synthesis in the lung, especially during systemic vitamin A insufficiency
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
all-trans-retinal suppresses liver, lung and testis bcmo1 expression, and 9-cis-retinal in lung and testis, in vitamin A-deficient rats
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BCM gene expression in the kidney of puromycin aminonucleoside-treated rats is increased
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BCM gene expression in the liver and intestines of puromycin aminonucleoside-treated rats is decreased
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chronic alcohol intake significantly upregulates hepatic BCMO1 expression in rats, possibly mediated via PPAR-gamma
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exposure to beta-carotene suppresses CMO1 expression at both mRNA and protein levels. beta-Carotene, but not all-trans retinoic acid, decreases CMO1 promoter activity in a time- and dosage-dependent manner. This beta-carotene-mediated inhibition of CMO1 expression results from decreased binding of peroxisome proliferator-activated receptor gamma and retinoid X receptor alpha in the CMO1 promoter
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intestinal BCM gene expresssion is increased in obese and dyslipedemic rats
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Isx, intestine specific homeobox, participates in the maintenance of vitamin A by regulating Bcmo1 expression in the intestine
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severe vitamin A deficiency markedly decreases intestine-specific transcription factor intestine-specific homeobox expression accompanied by an increase in BCMO1 expression in duodenum and jejunum
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