β-carotene 15,15'-monooxygenase
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enzymology An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different mol ...
, beta-carotene 15,15'-dioxygenase, () is an
enzyme An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different mol ...
with
systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ...
''beta-carotene:oxygen 15,15'-dioxygenase (bond-cleaving)''. In human it is encoded by the ''BCO1'' gene. This enzyme catalyses the following
chemical reaction A chemical reaction is a process that leads to the chemistry, chemical transformation of one set of chemical substances to another. When chemical reactions occur, the atoms are rearranged and the reaction is accompanied by an Gibbs free energy, ...
: beta-carotene + O2 → 2 all-''trans''-retinal This is a cleavage reaction which cleaves β-carotene, utilizes molecular oxygen, is enhanced by the presence of
bile salts Bile acids are steroid acids found predominantly in the bile of mammals and other vertebrates. Diverse bile acids are synthesized in the liver in peroxisomes. Bile acids are conjugated with taurine or glycine residues to give anions called bile ...
and
thyroxine Thyroxine, also known as T4, is a hormone produced by the thyroid gland. It is the primary form of thyroid hormone found in the blood and acts as a prohormone of the more active thyroid hormone, triiodothyronine (T3). Thyroxine and its acti ...
, and generates two molecules of
retinal Retinal (also known as retinaldehyde) is a polyene chromophore. Retinal, bound to proteins called opsins, is the chemical basis of visual phototransduction, the light-detection stage of visual perception (vision). Some microorganisms use ret ...
. In humans, the enzyme is present in the small intestine and liver. The dioxygenase also asymmetrically cleaves beta-cryptoxanthin, ''trans''-β-apo-8'-carotenal, beta-4'-apo-β-carotenal, alpha-carotene and gamma-carotene in decreasing order, creating one retinal molecule, all of these being substrates with a carbon chain greater than C30, with at least one unsubstituted
β-ionone The ionones, from greek ἴον ion "violet", are a series of closely related chemical substances that are part of a group of compounds known as rose ketones, which also includes damascones and damascenones. Ionones are aroma compounds found ...
ring. This enzyme belongs to the (enzymatically-defined) family of
oxidoreductase In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually ut ...
s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. A related enzyme is β-carotene 15,15'-monooxygenase, coded for by the gene BCMO1, which symmetrically cleaves β-carotene into two retinal molecules. In general, carnivores are poor converters of ionone-containing carotenoids, and pure carnivores such as felids (cats) lack beta-carotene 15,15'-dioxygenase and 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 belongs to the (similarity-defined) family of carotenoid oxygenases (). Enzymes of this family contain a Fe2+ active site, coordinated usually by four His residues.


References

EC 1.13.11 Iron enzymes Enzymes of unknown structure {{1.13-enzyme-stub