In enzymology, β-carotene 15,15'-dioxygenase (EC 22.214.171.124) is an enzyme with systematic name beta-carotene:oxygen 15,15'-dioxygenase (bond-cleaving). In human it is encoded by the BCO1 gene. This enzyme catalyses the following chemical reaction
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
|, BCDO, BCDO1, BCMO, BCMO1, BCO, beta-carotene oxygenase 1|
This is a cleavage reaction which cleaves β-carotene, utilizes molecular oxygen, is enhanced by the presence of bile salts and thyroxine, and generates two molecules of retinal. In humans, the enzyme is present in the small intestine and liver. It can also cleave beta-cryptoxanthin, apocarotenal, 4'-apo-β-carotenal, alpha-carotene and γ-carotene in decreasing order, all subtrates greater than C30 with at least one unsubstituted β-ionone ring.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. Other names in common use include β-carotene 15,15'-monooxygenase and β-carotene dioxygenase. Its previous EC numbers include 126.96.36.199 (1975), 188.8.131.52 (2001).
In general, carnivores are poor converters of ionone-containing carotenoids, and pure carnivores such as cats and ferrets lack beta-carotene 15,15'-monooxygenase and cannot convert any carotenoids to retinal (resulting in none of the carotenoids being forms of vitamin A for these species). They must have preformed vitamin A in their diet.
Beta-carotene 15,15'-dioxygenase contains Fe2+.
- GRCh38: Ensembl release 89: ENSG00000135697 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000031845 - Ensembl, May 2017
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- Kim YS, Kim NH, Yeom SJ, Kim SW, Oh DK (June 2009). "In vitro characterization of a recombinant Blh protein from an uncultured marine bacterium as a beta-carotene 15,15'-dioxygenase". The Journal of Biological Chemistry. 284 (23): 15781–93. doi:10.1074/jbc.M109.002618. PMC 2708875. PMID 19366683.
- Kim YS, Park CS, Oh DK (July 2010). "Retinal production from beta-carotene by beta-carotene 15,15'-dioxygenase from an unculturable marine bacterium". Biotechnology Letters. 32 (7): 957–61. doi:10.1007/s10529-010-0239-3. PMID 20229064.
- During A, Smith MK, Piper JB, Smith JC (November 2001). "beta-Carotene 15,15'-Dioxygenase activity in human tissues and cells: evidence of an iron dependency". The Journal of Nutritional Biochemistry. 12 (11): 640–647. doi:10.1016/s0955-2863(01)00184-x. PMID 12031257.
- Kim YS, Oh DK (March 2009). "Substrate specificity of a recombinant chicken beta-carotene 15,15'-monooxygenase that converts beta-carotene into retinal". Biotechnology Letters. 31 (3): 403–8. doi:10.1007/s10529-008-9873-4. PMID 18979213.
- Leuenberger MG, Engeloch-Jarret C, Woggon WD (2001). "The reaction mechanism of the enzyme-catalysed central cleavage of beta-carotene to retinal". Angew. Chem. 40: 2614–2616. doi:10.1002/1521-3773(20010716)40:14<2613::aid-anie2613>3.0.co;2-z.
- Goodman DS, Huang HS, Kanai M, Shiratori T (1967). "The enzymatic conversion of all-trans beta-carotene into retinal". J. Biol. Chem. 242: 3543–3554.
- Goodman DS, Huang HS, Shiratori T (May 1966). "Mechanism of the biosynthesis of vitamin A from beta-carotene". The Journal of Biological Chemistry. 241 (9): 1929–32. PMID 5946623.
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