EC |
1.13.11.63 |
Accepted name: |
β-carotene 15,15′-dioxygenase |
Reaction: |
β-carotene + O2 = 2 all-trans-retinal |
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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 |
References: |
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 24668807] |
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[EC 1.13.11.63 created 2012 (EC 1.14.99.36 created 1972 as EC 1.13.11.21, transferred 2001 to EC 1.14.99.36, incorporated 2015), modified 2016] |
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EC |
1.13.11.68 |
Accepted name: |
9-cis-β-carotene 9′,10′-cleaving dioxygenase |
Reaction: |
9-cis-β-carotene + O2 = 9-cis-10′-apo-β-carotenal + β-ionone |
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For diagram of strigol biosynthesis, click here |
Glossary: |
β-ionone = (3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one |
Other name(s): |
CCD7 (gene name); MAX3 (gene name); NCED7 (gene name) |
Systematic name: |
9-cis-β-carotene:oxygen oxidoreductase (9′,10′-cleaving) |
Comments: |
Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Booker, J., Auldridge, M., Wills, S., McCarty, D., Klee, H. and Leyser, O. MAX3/CCD7 is a carotenoid cleavage dioxygenase required for the synthesis of a novel plant signaling molecule. Curr. Biol. 14 (2004) 1232–1238. [DOI] [PMID: 15268852] |
2. |
Alder, A., Jamil, M., Marzorati, M., Bruno, M., Vermathen, M., Bigler, P., Ghisla, S., Bouwmeester, H., Beyer, P. and Al-Babili, S. The path from β-carotene to carlactone, a strigolactone-like plant hormone. Science 335 (2012) 1348–1351. [DOI] [PMID: 22422982] |
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[EC 1.13.11.68 created 2012] |
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EC |
1.13.11.71 |
Accepted name: |
carotenoid-9′,10′-cleaving dioxygenase |
Reaction: |
all-trans-β-carotene + O2 = all-trans-10′-apo-β-carotenal + β-ionone |
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For diagram of 10′-apo-β-carotenal biosynthesis, click here |
Other name(s): |
BCO2 (gene name); β-carotene 9′,10′-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9′,10′-cleaving) |
Systematic name: |
all-trans-β-carotene:oxygen oxidoreductase (9′,10′-cleaving) |
Comments: |
Requires Fe2+. The enzyme catalyses the asymmetric oxidative cleavage of carotenoids. The mammalian enzyme can also cleave all-trans-lycopene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kiefer, C., Hessel, S., Lampert, J.M., Vogt, K., Lederer, M.O., Breithaupt, D.E. and von Lintig, J. Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A. J. Biol. Chem. 276 (2001) 14110–14116. [DOI] [PMID: 11278918] |
2. |
Lindqvist, A., He, Y.G. and Andersson, S. Cell type-specific expression of β-carotene 9′,10′-monooxygenase in human tissues. J. Histochem. Cytochem. 53 (2005) 1403–1412. [DOI] [PMID: 15983114] |
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[EC 1.13.11.71 created 2012] |
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