Carotenoid oxygenase

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Retinal pigment epithelial membrane protein
[[File:PDB 2biw
Crystal structure of Synechocystis ACO.png
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The Structure of a Retinal-Forming Carotenoid Oxygenase. [1]
Identifiers
SymbolRPE65
Pfam PF03055
InterPro IPR004294
SCOP2 2biw / SCOPe / SUPFAM
OPM superfamily 103
OPM protein 2biw
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Carotenoid oxygenases are a family of enzymes involved in the cleavage of carotenoids to produce, for example, retinol, commonly known as vitamin A. This family includes an enzyme known as RPE65 which is abundantly expressed in the retinal pigment epithelium where it catalyzed the formation of 11-cis-retinol from all-trans-retinyl esters.

Contents

The RPE65 iron(II) cofactor, showing its coordination with 4 histidine residues and 3 glutamic acid residues. RPE65 Active Site.png
The RPE65 iron(II) cofactor, showing its coordination with 4 histidine residues and 3 glutamic acid residues.

Carotenoids such as beta-carotene, lycopene, lutein and beta-cryptoxanthin are produced in plants and certain bacteria, algae and fungi, where they function as accessory photosynthetic pigments and as scavengers of oxygen radicals for photoprotection. They are also essential dietary nutrients in animals. Carotenoid oxygenases cleave a variety of carotenoids into a range of biologically important products, including apocarotenoids in plants that function as hormones, pigments, flavours, floral scents and defence compounds, and retinoids in animals that function as vitamins, chromophores for opsins and signalling molecules. [3] Examples of carotenoid oxygenases include:

Members of the family use an iron(II) active center, usually held by four histidines.

Human proteins containing this domain

BCO2; BCO1; RPE65;

Related Research Articles

<span class="mw-page-title-main">Carotene</span> Class of compounds

The term carotene (also carotin, from the Latin carota, "carrot") is used for many related unsaturated hydrocarbon substances having the formula C40Hx, which are synthesized by plants but in general cannot be made by animals (with the exception of some aphids and spider mites which acquired the synthesizing genes from fungi). Carotenes are photosynthetic pigments important for photosynthesis. Carotenes contain no oxygen atoms. They absorb ultraviolet, violet, and blue light and scatter orange or red light, and (in low concentrations) yellow light.

<span class="mw-page-title-main">Vitamin A</span> Essential nutrient

Vitamin A is a fat-soluble vitamin and an essential nutrient for animals. The term "vitamin A" encompasses a group of chemically related organic compounds that includes retinol, retinal, retinoic acid, and several provitamin (precursor) carotenoids, most notably beta-carotene. Vitamin A has multiple functions: it is essential for embryo development and growth, for maintenance of the immune system, and for vision, where it combines with the protein opsin to form rhodopsin – the light-absorbing molecule necessary for both low-light and color vision.

<span class="mw-page-title-main">Retinol</span> Chemical compound

Retinol, also called vitamin A1, is a fat-soluble vitamin in the vitamin A family that is found in food and used as a dietary supplement. Retinol or other forms of vitamin A are needed for vision, cellular development, maintenance of skin and mucous membranes, immune function and reproductive development. Dietary sources include fish, dairy products, and meat. As a supplement it is used to treat and prevent vitamin A deficiency, especially that which results in xerophthalmia. It is taken by mouth or by injection into a muscle. As an ingredient in skin-care products, it is used to reduce wrinkles and other effects of skin aging.

<span class="mw-page-title-main">Carotenoid</span> Class of chemical compounds; yellow, orange or red plant pigments

Carotenoids are yellow, orange, and red organic pigments that are produced by plants and algae, as well as several bacteria, archaea, and fungi. Carotenoids give the characteristic color to pumpkins, carrots, parsnips, corn, tomatoes, canaries, flamingos, salmon, lobster, shrimp, and daffodils. Over 1,100 identified carotenoids can be further categorized into two classes – xanthophylls and carotenes.

β-Carotene Red-orange pigment of the terpenoids class

β-Carotene (beta-carotene) is an organic, strongly colored red-orange pigment abundant in fungi, plants, and fruits. It is a member of the carotenes, which are terpenoids (isoprenoids), synthesized biochemically from eight isoprene units and thus having 40 carbons.

<span class="mw-page-title-main">Retinal</span> Chemical compound

Retinal 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).

γ-Carotene (gamma-carotene) is a carotenoid, and is a biosynthetic intermediate for cyclized carotenoid synthesis in plants. It is formed from cyclization of lycopene by lycopene cyclase epsilon. Along with several other carotenoids, γ-carotene is a vitamer of vitamin A in herbivores and omnivores. Carotenoids with a cyclized, beta-ionone ring can be converted to vitamin A, also known as retinol, by the enzyme beta-carotene 15,15'-dioxygenase; however, the bioconversion of γ-carotene to retinol has not been well-characterized. γ-Carotene has tentatively been identified as a biomarker for green and purple sulfur bacteria in a sample from the 1.640 ± 0.003-Gyr-old Barney Creek Formation in Northern Australia which comprises marine sediments. Tentative discovery of γ-carotene in marine sediments implies a past euxinic environment, where water columns were anoxic and sulfidic. This is significant for reconstructing past oceanic conditions, but so far γ-carotene has only been potentially identified in the one measured sample.

The visual cycle is a process in the retina that replenishes the molecule retinal for its use in vision. Retinal is the chromophore of most visual opsins, meaning it captures the photons to begin the phototransduction cascade. When the photon is absorbed, the 11-cis retinal photoisomerizes into all-trans retinal as it is ejected from the opsin protein. Each molecule of retinal must travel from the photoreceptor cell to the RPE and back in order to be refreshed and combined with another opsin. This closed enzymatic pathway of 11-cis retinal is sometimes called Wald's visual cycle after George Wald (1906–1997), who received the Nobel Prize in 1967 for his work towards its discovery.

In enzymology, a retinol dehydrogenase (RDH) (EC 1.1.1.105) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Beta-carotene 15,15'-dioxygenase</span> Mammalian protein found in Homo sapiens

In enzymology, beta-carotene 15,15'-dioxygenase, (EC 1.13.11.63) 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

Apo-beta-carotenoid-14',13'-dioxygenase (EC 1.13.11.67 is an enzyme that catalyzes the chemical reaction

In enzymology, a retinol isomerase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">RPE65</span> Protein-coding gene in humans

Retinal pigment epithelium-specific 65 kDa protein is a retinoid isomerohydrolase enzyme of the vertebrate visual cycle. RPE65 is expressed in the retinal pigment epithelium and is responsible for the conversion of all-trans-retinyl esters to 11-cis-retinol during phototransduction. 11-cis-retinol is then used in visual pigment regeneration in photoreceptor cells. RPE65 belongs to the carotenoid oxygenase family of enzymes.

Apocarotenoids are organic compounds which occur widely in living organisms. They are derived from carotenoids by oxidative cleavage, catalyzed by carotenoid oxygenases. Examples include the vitamin A retinoids retinal, retinoic acid, and retinol; and the plant hormone abscisic acid.

Phytoene desaturase (3,4-didehydrolycopene-forming) is an enzyme with systematic name 15-cis-phytoene:acceptor oxidoreductase (3,4-didehydrolycopene-forming). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Phytoene desaturase (lycopene-forming)</span>

Phytoene desaturase (lycopene-forming) are enzymes found in archaea, bacteria and fungi that are involved in carotenoid biosynthesis. They catalyze the conversion of colorless 15-cis-phytoene into a bright red lycopene in a biochemical pathway called the poly-trans pathway. The same process in plants and cyanobacteria utilizes four separate enzymes in a poly-cis pathway.

Torulene dioxygenase (EC 1.13.11.59, CAO-2, CarT) is an enzyme with systematic name torulene:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction

9-cis-beta-carotene 9',10'-cleaving dioxygenase (EC 1.13.11.68, CCD7 (gene), MAX3 (gene), NCED7 (gene)) is an enzyme with systematic name 9-cis-beta-carotene:O2 oxidoreductase (9',10'-cleaving). This enzyme catalyses the following chemical reaction

Carotenoid-9',10'-cleaving dioxygenase (EC 1.13.11.71, BCO2 (gene), beta-carotene 9',10'-monooxygenase (misleading)) is an enzyme with systematic name all-trans-beta-carotene:O2 oxidoreductase (9',10'-cleaving). This enzyme catalyses the following chemical reaction

All-trans-8'-apo-beta-carotenal 15,15'-oxygenase (EC 1.14.99.41, Diox1, ACO, 8'-apo-beta-carotenal 15,15'-oxygenase) is an enzyme with systematic name all-trans-8'-apo-beta-carotenal:oxygen 15,15'-oxidoreductase (bond-cleaving). This enzyme catalyses the following chemical reaction

References

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  2. Kiser PD, Zhang J, Badiee M, Li Q, Shi W, Sui X, et al. (June 2015). "Catalytic mechanism of a retinoid isomerase essential for vertebrate vision". Nature Chemical Biology. 11 (6): 409–15. doi:10.1038/nchembio.1799. PMC   4433804 . PMID   25894083.
  3. 1 2 3 Wyss A (January 2004). "Carotene oxygenases: a new family of double bond cleavage enzymes". The Journal of Nutrition. 134 (1): 246S–250S. doi: 10.1093/jn/134.1.246S . PMID   14704328.
  4. Tan BC, Joseph LM, Deng WT, Liu L, Li QB, Cline K, McCarty DR (July 2003). "Molecular characterization of the Arabidopsis 9-cis epoxycarotenoid dioxygenase gene family". The Plant Journal. 35 (1): 44–56. doi: 10.1046/j.1365-313X.2003.01786.x . PMID   12834401.
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Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR004294