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Information on EC 1.14.99.36 - beta-carotene 15,15'-monooxygenase and Organism(s) Homo sapiens and UniProt Accession Q9HAY6
for references in articles please use BRENDA:EC1.14.99.36deleted. Now classified as EC 1.13.11.63, beta-carotene 15,15'-dioxygenase
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1.14.99.36 beta-carotene 15,15'-monooxygenaseSynonyms
beta-carotene 15,15'-dioxygenase, 
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topkcat/KM VALUE [1/mMs-1] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.1016
beta-carotene
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recombinant His6-tagged enzyme, pH and temperature not specified in the publication
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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BCMO1 is a member of an evolutionary well-conserved family of carotenoid cleavage oxygenases
malfunction
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transfection of cells with BCMO1 siRNA inhibits BCMO1 expression, enhances cancer migration and invasion, and increases expression of MMP7 and MMP28
metabolism
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beta-carotene 15,15'-monooxygenase is a key enzyme in vitamin A metabolism
physiological function
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
physiological function
additional information
physiological function
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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
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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
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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
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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
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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
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carotenoid 15,15'-oxygenases produce retinal from carotenoids
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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