All-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase

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All-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase
Identifiers
EC no. 1.13.11.70
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All-trans-10'-apo-beta-carotenal 13,14-cleaving dioxygenase (EC 1.13.11.70, CCD8 (gene), MAX4 (gene), NCED8 (gene)) is an enzyme with systematic name all-trans-10'-apo-beta-carotenal:O2 oxidoreductase (13,14-cleaving). [1] This enzyme catalyses the following chemical reaction

all-trans-10'-apo-beta-carotenal + O2 13-apo-beta-carotenone + (2E,4E,6E)-4-methylocta-2,4,6-trienedial

The enzyme contains Fe2+.

Related Research Articles

<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">Apocarotenal</span> Chemical compound

Apocarotenal, or trans-β-apo-8'-carotenal, is a carotenoid found in spinach and citrus fruits. Like other carotenoids, apocarotenal plays a role as a precursor of vitamin A, even though it has 50% less pro-vitamin A activity than β-carotene. The empirical chemical formula for apocarotenal is C30H40O.

<span class="mw-page-title-main">Carotenoid oxygenase</span>

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.

<span class="mw-page-title-main">Homogentisate 1,2-dioxygenase</span> Enzyme

Homogentisate 1,2-dioxygenase (homogentisic acid oxidase, homogentisate oxidase, homogentisicase) is an enzyme which catalyzes the conversion of homogentisate to 4-maleylacetoacetate. Homogentisate 1,2-dioxygenase or HGD is involved in the catabolism of aromatic rings, more specifically in the breakdown of the amino acids tyrosine and phenylalanine. HGD appears in the metabolic pathway of tyrosine and phenylalanine degradation once the molecule homogentisate is produced. Homogentisate reacts with HGD to produce maleylacetoacetate, which then is further used in the metabolic pathway. HGD requires the use of Fe2+ and O2 in order to cleave the aromatic ring of homogentisate.

<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 BCDO2 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

Beta-apo-4'-carotenal oxygenase (EC 1.2.1.82, beta-apo-4'-carotenal dehydrogenase, YLO-1, carD (gene)) is an enzyme with systematic name 4'-apo-beta,psi-carotenal:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction:

<span class="mw-page-title-main">9-cis-epoxycarotenoid dioxygenase</span> Class of enzymes

9-cis-epoxycarotenoid dioxygenase (EC 1.13.11.51, nine-cis-epoxycarotenoid dioxygenase, NCED, AtNCED3, PvNCED1, VP14) is an enzyme in the biosynthesis of abscisic acid (ABA), with systematic name 9-cis-epoxycarotenoid 11,12-dioxygenase. This enzyme catalyses the following chemical reaction

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

Carotenoid isomerooxygenase (EC 1.13.11.65, ninaB (gene)) is an enzyme with systematic name zeaxanthin:oxygen 15,15'-oxidoreductase (bond-cleaving, cis-isomerizing). This enzyme catalyses the following chemical reaction

8'-apo-beta-carotenoid 14',13'-cleaving dioxygenase (EC 1.13.11.67) is an enzyme with systematic name 8'-apo-beta-carotenol:O2 oxidoreductase (14',13'-cleaving). 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

Carlactone synthase (EC 1.13.11.69, CCD8 (gene), MAX4 (gene), NCED8 (gene)) is an enzyme with systematic name 9-cis-10'-apo-beta-carotenal:O2 oxidoreductase (14,15-cleaving, carlactone-forming). This enzyme catalyses the following chemical reaction

CCD8 (gene) may refer to:

MAX4 (gene) may refer to:

NCED8 (gene) may refer to:

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

Zeaxanthin 7,8-dioxygenase (EC 1.14.99.42, zeaxanthin 7,8(7',8')-cleavage dioxygenase, CsZCD) is an enzyme with systematic name zeaxanthin:oxygen oxidoreductase (7,8-cleaving). This enzyme catalyses the following chemical reaction

References

  1. Schwartz SH, Qin X, Loewen MC (November 2004). "The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching" (PDF). The Journal of Biological Chemistry. 279 (45): 46940–5. doi: 10.1074/jbc.M409004200 . PMID   15342640.