Beta-carotene 15,15'-monooxygenase

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In enzymology, a beta-carotene 15,15'-monooxygenase (EC 1.14.99.36) is an enzyme that catalyzes the chemical reaction

beta-carotene + O₂ $\rightleftharpoons$ 2 retinal

Thus, the two substrates of this enzyme are beta-carotene and O₂, whereas its product is retinal.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is beta-carotene:oxygen 15,15'-oxidoreductase (bond-cleaving). Other names in common use include beta-carotene 15,15'-dioxygenase, carotene dioxygenase, and carotene 15,15'-dioxygenase. This enzyme participates in retinol metabolism. It has 2 cofactors: iron, and Bile salt.

[edit] References

IUBMB entry for 1.14.99.36
BRENDA references for 1.14.99.36 (Recommended.)
PubMed references for 1.14.99.36
PubMed Central references for 1.14.99.36
Google Scholar references for 1.14.99.36
Leuenberger MG, Engeloch-Jarret C and Woggon WD (2001). "The reaction mechanism of the enzyme-catalysed central cleavage of beta-carotene to retinal". Angew. Chem. 40: 2614–2616.
Goodman DS, Huang HS, Kanai M and 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 (1966). "Mechanism of the biosynthesis of vitamin A from beta-carotene". J. Biol. Chem. 241: 1929–32. PMID 5946623.