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Enzyme Nomenclature
Information on EC 1.14.99.45 - carotene epsilon-monooxygenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.99.45
-
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RECOMMENDED NAME
GeneOntology No.
carotene epsilon-monooxygenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-carotene + AH2 + O2 = alpha-cryptoxanthin + A + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
alpha-carotene:oxygen oxidoreductase (3-hydroxylating)
A heme-thiolate protein (P-450). Also acts on zeinoxanthin to give lutein.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
mis-expressing of CYP97C1 impacts carotenoids metabolic flux
malfunction
quadruple chy1chy2lut2lut5 mutant lacks lutein and shows a compensatory increase in beta-xanthophylls with respect to the chy1chy2lut5 mutant. Chy1chy2lut2lut5 mutant plants show an even stronger photosensitivity than mutant chy1chy2lut5, a complete lack of qE, the rapidly reversible component of non-photochemical quenching, and a peculiar organization of the pigment binding complexes into thylakoids. The chy1chy2lut2lut5 mutant is depleted in Lhcb subunits and is specifically affected in Photosystem I function, showing a deficiency in PSI-LHCI supercomplexes, phenotype, overview; quadruple chy1chy2lut2lut5 mutant lacks lutein and shows a compensatory increase in beta-xanthophylls with respect to the chy1chy2lut5 mutant. Chy1chy2lut2lut5 mutant plants show an even stronger photosensitivity than mutant chy1chy2lut5, a complete lack of qE, the rapidly reversible component of non-photochemical quenching, and a peculiar organization of the pigment binding complexes into thylakoids. The chy1chy2lut2lut5 mutant is depleted in Lhcb subunits and is specifically affected in Photosystem I function, showing a deficiency in PSI-LHCI supercomplexes, phenotype, overview
metabolism
the first step in xanthophyll biosynthesis from alpha- and beta-carotene is the hydroxylation of epsilon- and beta-rings, performed by both non-heme iron oxygenases CHY1 and CHY2, and by P450 cytochromes, LUT1/CYP97C1 and LUT5/CYP97A3. CHY1, CHY2, LUT1/CYP97C1 and LUT5/CYP97A3 are the complete complement of carotene hydroxylases in Arabidopsis thaliana; the first step in xanthophyll biosynthesis from alpha- and beta-carotene is the hydroxylation of epsilon- and beta-rings, performed by both non-heme iron oxygenases CHY1 and CHY2, and by P450 cytochromes, LUT1/CYP97C1 and LUT5/CYP97A3. CHY1, CHY2, LUT1/CYP97C1 and LUT5/CYP97A3 are the complete complement of carotene hydroxylases in Arabidopsis thaliana
metabolism
BT012891
the enzyme is involved in the biosynthetic pathway of lutein in plants, overview
physiological function
the enzyme is involved in xanthophyll biosynthesis, correlation between xanthophyll levels and the PSI-PSII ratio, xanthophylls are needed for normal level of Photosystem I and LHCII accumulation; the enzyme is involved in xanthophyll biosynthesis, correlation between xanthophyll levels and the PSI-PSII ratio, xanthophylls are needed for normal level of Photosystem I and LHCII accumulation
physiological function
BT012891
the overexpression of gene LeLUT1 has a key function in alleviating photoinhibition and photooxidation, and decreases the sensitivity of photosynthesis to chilling stress
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-carotene + AH2 + O2
alpha-cryptoxanthin + A + H2O
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CYP97C1 has alpha-carotene epsilon-ring hydroxylase activity
-
-
?
alpha-carotene + reduced cytochrome P40 + O2
lutein + oxidized cytochrome P40 + H2O
-
-
-
?
beta-carotene + reduced cytochrome P40 + O2
zeaxanthin + oxidized cytochrome P40 + H2O
-
-
-
?
zeinoxanthin + AH2 + O2
lutein + A + H2O
-
-
-
-
?
additional information
?
-
-
CYP97C1 catalyzes hydroxylation of the epsilon-ring of beta,epsilon-carotenoids
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-
-
additional information
?
-
LUT1/CYP97C1 protein reveals a major beta-carotene hydroxylase activity in vivo when depleted in its preferred substrate alpha-carotene
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-
-
additional information
?
-
LUT1/CYP97C1 protein reveals a major beta-carotene hydroxylase activity in vivo when depleted in its preferred substrate alpha-carotene
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-carotene + reduced cytochrome P40 + O2
lutein + oxidized cytochrome P40 + H2O
Q6TBX7, Q93VK5
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-
-
?
beta-carotene + reduced cytochrome P40 + O2
zeaxanthin + oxidized cytochrome P40 + H2O
Q6TBX7, Q93VK5
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-
-
?
additional information
?
-
Q6TBX7
LUT1/CYP97C1 protein reveals a major beta-carotene hydroxylase activity in vivo when depleted in its preferred substrate alpha-carotene
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-
-
additional information
?
-
Q93VK5
LUT1/CYP97C1 protein reveals a major beta-carotene hydroxylase activity in vivo when depleted in its preferred substrate alpha-carotene
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
a heme-containing cytochrome P450 enzyme; a heme-containing cytochrome P450 enzyme
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
BT012891
expression of LeLUT1 is the highest in the leaves in tomato
additional information
BT012891
expression pattern in various tomato organs, quantitative expression analysis, overview
additional information
-
expression pattern in various tomato organs, quantitative expression analysis, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene LeLUT1, DNA and amino acid sequence determination and analysis, quantitative RT-PCR expression analysis, expression of gene LeLUT1-GFP fusion protein in chloroplasts of Arabidopsis thaliana mesophyll protoplasts, quantitative real-time PCR expression analysis
BT012891
genes lut1 and lut5, real-time PCR expression analysis; genes lut1 and lut5, real-time PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of LeLUT1 is downregulated by various abiotic stresses in tomato
BT012891
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of the triple chy1chy2lut5 mutant, which is almost completely depleted in beta-xanthophylls. Quadruple chy1chy2lut2lut5 mutant, additionally carrying the lut2 mutation (affecting lycopene epsilon-cyclase) lacks lutein and shows a compensatory increase in beta-xanthophylls with respect to chy1chy2lut5 mutant. Leaf carotenoid contents of wild-type and mutant enzymes, overview; construction of the triple chy1chy2lut5 mutant, which is almost completely depleted in beta-xanthophylls. Quadruple chy1chy2lut2lut5 mutant, additionally carrying the lut2 mutation (affecting lycopene epsilon-cyclase) lacks lutein and shows a compensatory increase in beta-xanthophylls with respect to chy1chy2lut5 mutant. Leaf carotenoid contents of wild-type and mutant enzymes, overview
additional information
construction of the triple chy1chy2lut5 mutant, which is almost completely depleted in beta-xanthophylls. Quadruple chy1chy2lut2lut5 mutant, additionally carrying the lut2 mutation (affecting lycopene epsilon-cyclase) lacks lutein and shows a compensatory increase in beta-xanthophylls with respect to chy1chy2lut5 mutant. Leaf carotenoid contents of wild-type and mutant enzymes, overview; construction of the triple chy1chy2lut5 mutant, which is almost completely depleted in beta-xanthophylls. Quadruple chy1chy2lut2lut5 mutant, additionally carrying the lut2 mutation (affecting lycopene epsilon-cyclase) lacks lutein and shows a compensatory increase in beta-xanthophylls with respect to chy1chy2lut5 mutant. Leaf carotenoid contents of wild-type and mutant enzymes, overview
additional information
BT012891
construction of transgenic Nicotiana tabacum plants overexpressing LeLUT1, the transgenic plants have a higher lutein content, which is decreased in cold condition. Under chilling stress, the non-photochemical quenching values are higher in the transgenic plants than in the wild-type plants. Compared with the wild-type plants, the transgenic plants show lower levels of hydrogen peroxide, superoxide radical, relative electrical conductivity, and malondialdehyde content, and relatively higher values of maximal photochemical efficiency of photosystem II, oxidizable P700 of PSI, and net photosynthetic rate. The transgenic seedlings are less suppressed in growth and lose less cotyledon chlorophyll than the wild-type seedlings
additional information
-
construction of transgenic Nicotiana tabacum plants overexpressing LeLUT1, the transgenic plants have a higher lutein content, which is decreased in cold condition. Under chilling stress, the non-photochemical quenching values are higher in the transgenic plants than in the wild-type plants. Compared with the wild-type plants, the transgenic plants show lower levels of hydrogen peroxide, superoxide radical, relative electrical conductivity, and malondialdehyde content, and relatively higher values of maximal photochemical efficiency of photosystem II, oxidizable P700 of PSI, and net photosynthetic rate. The transgenic seedlings are less suppressed in growth and lose less cotyledon chlorophyll than the wild-type seedlings
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.45)
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