The Enzyme Database

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Accepted name: β-carotene 15,15′-dioxygenase
Reaction: β-carotene + O2 = 2 all-trans-retinal
For diagram of retinal and derivatives biosynthesis, click here
Other name(s): blh (gene name); BCO1 (gene name); BCDO (gene name); carotene dioxygenase; carotene 15,15′-dioxygenase; BCMO1 (misleading); β-carotene 15,15′-monooxygenase (incorrect)
Systematic name: β-carotene:oxygen 15,15′-dioxygenase (bond-cleaving)
Comments: Requires Fe2+. The enzyme cleaves β-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products [8]. The enzyme can also process β-cryptoxanthin, 8′-apo-β-carotenal, 4′-apo-β-carotenal, α-carotene and γ-carotene in decreasing order. The presence of at least one unsubstituted β-ionone ring in a substrate greater than C30 is mandatory [5]. A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore [6,7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Goodman, D.S., Huang, H.S. and Shiratori, T. Mechanism of the biosynthesis of vitamin A from β-carotene. J. Biol. Chem. 241 (1966) 1929–1932. [PMID: 5946623]
2.  Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T. The enzymatic conversion of all-trans β-carotene into retinal. J. Biol. Chem. 242 (1967) 3543–3554.
3.  Yan, W., Jang, G.F., Haeseleer, F., Esumi, N., Chang, J., Kerrigan, M., Campochiaro, M., Campochiaro, P., Palczewski, K. and Zack, D.J. Cloning and characterization of a human β,β-carotene-15,15′-dioxygenase that is highly expressed in the retinal pigment epithelium. Genomics 72 (2001) 193–202. [PMID: 11401432]
4.  Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D. The reaction mechanism of the enzyme-catalysed central cleavage of β-carotene to retinal. Angew. Chem. 40 (2001) 2614–2616. [PMID: 11458349]
5.  Kim, Y.S. and Oh, D.K. Substrate specificity of a recombinant chicken β-carotene 15,15′-monooxygenase that converts β-carotene into retinal. Biotechnol. Lett. 31 (2009) 403–408. [PMID: 18979213]
6.  Kim, Y.S., Kim, N.H., Yeom, S.J., Kim, S.W. and Oh, D.K. In vitro characterization of a recombinant Blh protein from an uncultured marine bacterium as a β-carotene 15,15′-dioxygenase. J. Biol. Chem. 284 (2009) 15781–15793. [PMID: 19366683]
7.  Kim, Y.S., Park, C.S. and Oh, D.K. Retinal production from β-carotene by β-carotene 15,15′-dioxygenase from an unculturable marine bacterium. Biotechnol. Lett. 32 (2010) 957–961. [PMID: 20229064]
8.  dela Seña, C., Riedl, K.M., Narayanasamy, S., Curley, R.W., Jr., Schwartz, S.J. and Harrison, E.H. The human enzyme that converts dietary provitamin A carotenoids to vitamin A is a dioxygenase. J. Biol. Chem. 289 (2014) 13661–13666. [PMID: 24668807]
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