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Information on EC 1.14.14.158 - carotenoid epsilon hydroxylase
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1.14.14.158 carotenoid epsilon hydroxylaseIUBMB Comments
A heme-thiolate protein (P-450). Also acts on zeinoxanthin to give lutein.
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Word Map
- 1.14.14.158
- lutein
- elongase
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xanthophylls
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light-harvesting
- chlorophyll
-
p450-type
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photoprotection
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photooxidation
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vlcfas
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non-heme
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very-long-chain
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hydroxylases
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ripening
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drought
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di-iron
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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Synonyms
carotenoid epsilon-ring hydroxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carotenoid epsilon hydroxylase
carotenoid epsilon-hydroxylase
carotenoid epsilon-ring hydroxylase
CYP97C
CYP97C1
CYP97C19
LUT1
CYP97C1
-
-
-
-
LUT1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-carotene + [reduced NADPH-hemoprotein reductase] + O2 = alpha-cryptoxanthin + [oxidized NADPH-hemoprotein reductase] + H2O
(1)
-
-
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zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2 = lutein + [oxidized NADPH-hemoprotein reductase] + H2O
(2)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
alpha-carotene,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
A heme-thiolate protein (P-450). Also acts on zeinoxanthin to give lutein.
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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 + [reduced NADPH-hemoprotein reductase] + O2
alpha-cryptoxanthin + [oxidized NADPH-hemoprotein reductase] + H2O
alpha-carotene + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
beta-carotene + reduced cytochrome P-450 + O2
zeaxanthin + oxidized cytochrome P-450 + H2O
-
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
alpha-carotene + [reduced NADPH-hemoprotein reductase] + O2
alpha-cryptoxanthin + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
alpha-carotene + [reduced NADPH-hemoprotein reductase] + O2
alpha-cryptoxanthin + [oxidized NADPH-hemoprotein reductase] + H2O
-
CYP97C1 has alpha-carotene epsilon-ring hydroxylase activity
-
-
?
alpha-carotene + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
alpha-carotene + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
recombinant enzyme
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
BT012891
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-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
maize CYP97C19 is an enzyme with strong zeinoxanthin epsilon-ring hydroxylation activity
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
Zea mays L. cv B73
maize CYP97C19 is an enzyme with strong zeinoxanthin epsilon-ring hydroxylation activity
-
-
?
additional information
?
-
-
CYP97C1 catalyzes hydroxylation of the epsilon-ring of beta,epsilon-carotenoids
-
-
-
additional information
?
-
LUT1/CYP97C1 protein reveals a major beta-carotene hydroxylase activity in vivo when depleted in its preferred substrate alpha-carotene
-
-
-
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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NATURAL SUBSTRATE
NATURAL 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 + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
beta-carotene + reduced cytochrome P-450 + O2
zeaxanthin + oxidized cytochrome P-450 + H2O
Q6TBX7, Q93VK5
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-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
alpha-carotene + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
Q6TBX7, Q93VK5
-
-
-
?
alpha-carotene + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
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-
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
A0A1L7NT18
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-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
BT012891
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-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
K9J9Z8
maize CYP97C19 is an enzyme with strong zeinoxanthin epsilon-ring hydroxylation activity
-
-
?
zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2
lutein + [oxidized NADPH-hemoprotein reductase] + H2O
Zea mays L. cv B73
K9J9Z8
maize CYP97C19 is an enzyme with strong zeinoxanthin epsilon-ring hydroxylation activity
-
-
?
additional information
?
-
Q6TBX7
LUT1/CYP97C1 protein reveals a major beta-carotene hydroxylase activity in vivo when depleted in its preferred substrate alpha-carotene
-
-
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in flavedo and juice sacs, expression of CitCYP97C increases with two peaks in September and November, respectively
brenda
additional information
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about 2.5fold higher expression compared to roots and flowers
brenda
BT012891
expression of LeLUT1 is the highest in the leaves in tomato
brenda
additional information
lutein content in the juice sacs during the ripening process is high during November and December, and in the flavedo it is highest in August, while lowest in December, overview
brenda
additional information
BT012891
expression pattern in various tomato organs, quantitative expression analysis, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
as most carotenoids are synthesized and stored in plastids, the location of CitCYP97C, together with the other enzymes involved, i.e. CitHYb, CitCYP97A, and CitCYP97B, within plastid allows them to catalyze the reaction of carotene hydroxylation
brenda
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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
metabolism
the enzyme is involved in the carotenoid biosynthesis pathway
metabolism
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the enzyme is involved in the carotenoid biosynthesis pathway, for which 7 crucial genes are responsible, 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
physiological function
of the four citrus carotene hydroxylases presented in four distinct clusters, CitCYP97C is the one responsible for epsilon-ring hydroxylation in Citrus unshiu, while CitCYP97A and CitCYP97B hydroxylate the alpha- and beta-rings of alpha-carotene, respectively, roles of four carotene hydroxylase genes (CitHYb, CitCYP97A, CitCYP97B, and CitCYP97C) in regulating xanthophylls biosynthesis. Zeaxanthin increases significantly during the ripening process in Citrus fruits, contents of alpha-carotene and lutein increase gradually in the juice sacs during the ripening process, the content of beta-cryptoxanthin, the major carotenoid in Satsuma mandarin, increases significantly during the ripening process in December, overview
physiological function
-
alpha-carotene and beta-carotene turns into lutein and zeaxanthin, respectively, by the hydroxylation process, in the presence of epsilon-ring carotene hydroxylase and beta-ring carotene hydroxylase
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Zea mays L. cv B73
-
x * 61900, about, sequence calculation of ZmCYP97C19
-
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PROTEIN VARIANTS
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
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression of CYP97C19 cDNA under the control of the constitutive CaMV 35S promoter in the Arabidopsis thaliana lut1 knockout mutant, which lacks a functional CYP97C1 (LUT1) gene; gene CYP97C19, cDNA is cloned from leaves, the ZmCYP97C19 gene has nine introns and ten exons, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic structure, overview. Functional recombinant expression under the control of constitutive CaMV 35S promoter in rosettes leaves of the Arabidopsis thaliana lut1 knockout mutant, which lacks a functional CYP97C1 (LUT1) gene. Lutein accumulates to high levels in the rosette leaves of the transgenic lines but not in the untransformed lut1 mutants, carotenoid extraction and quantification from Arabidopsis thaliana lut1-CYP97C1 leaves
gene CHXE, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, quantitative real-time PCR enzyme expression analysis
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gene CitCYP97C, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis. When CitHYb and CitCYP97C are coexpressed in Escherichia coli strain BL21(DE3) the monohydroxylated zeinoxanthin, which is produced by CitHYb, is further converted to lutein by CitCYP97C, when CitCYP97A and CitCYP97C are coexpressed or CitCYP97B and CitCYP97C are coexpressed, no hydroxylated carotene is detected in the alpha-carotene- and beta-carotene-accumulating Escherichia coli strain BL21(DE3) cells
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, J.; Cheng, K.; Craft, N.; Hamberger, B.; Douglas, C.
Over-expression of Arabidopsis thaliana carotenoid hydroxylases individually and in combination with a beta-carotene ketolase provides insight into in vivo functions
Phytochemistry
71
168-178
2010
Arabidopsis thaliana
brenda
Pogson, B.; McDonald, K.A.; Truong, M.; Britton, G.; DellaPenna, D.
Arabidopsis carotenoid mutants demonstrate that lutein is not essential for photosynthesis in higher plants
Plant Cell
8
1627-1639
1996
Arabidopsis thaliana
brenda
Tian, L.; Musetti, V.; Kim, J.; Magallanes-Lundback, M.; DellaPenna, D.
The Arabidopsis LUT1 locus encodes a member of the cytochrome p450 family that is required for carotenoid epsilon-ring hydroxylation activity
Proc. Natl. Acad. Sci. USA
101
402-407
2004
Arabidopsis thaliana
brenda
Kim, J.; DellaPenna, D.
Defining the primary route for lutein synthesis in plants: the role of Arabidopsis carotenoid beta-ring hydroxylase CYP97A3
Proc. Natl. Acad. Sci. USA
103
3474-3479
2006
Arabidopsis thaliana
brenda
Fiore, A.; DallOsto, L.; Cazzaniga, S.; Diretto, G.; Giuliano, G.; Bassi, R.
A quadruple mutant of Arabidopsis reveals a beta-carotene hydroxylation activity for LUT1/CYP97C1 and a regulatory role of xanthophylls on determination of the PSI/PSII ratio
BMC Plant Biol.
12
50
2012
Arabidopsis thaliana (Q6TBX7), Arabidopsis thaliana (Q93VK5)
brenda
Zhou, B.; Deng, Y.S.; Kong, F.Y.; Li, B.; Meng, Q.W.
Overexpression of a tomato carotenoid epsilon-hydroxylase gene alleviates sensitivity to chilling stress in transgenic tobacco
Plant Physiol. Biochem.
70
235-245
2013
Solanum lycopersicum (BT012891), Solanum lycopersicum
brenda
Ma, G.; Zhang, L.; Yungyuen, W.; Tsukamoto, I.; Iijima, N.; Oikawa, M.; Yamawaki, K.; Yahata, M.; Kato, M.
Expression and functional analysis of Citrus carotene hydroxylases unravelling the xanthophyll biosynthesis in citrus fruits
BMC Plant Biol.
16
148
2016
Citrus unshiu (A0A1L7NT18)
brenda
Reddy, C.S.; Lee, S.H.; Yoon, J.S.; Kim, J.K.; Lee, S.W.; Hur, M.; Koo, S.C.; Meilan, J.; Lee, W.M.; Jang, J.K.; Hur, Y.; Park, S.U.; Kim, A.Y.B.
Molecular cloning and characterization of carotenoid pathway genes and carotenoid content in Ixeris dentata var. albiflora
Molecules
22
E1449
2017
Ixeridium dentatum
brenda
Chang, S.; Berman, J.; Sheng, Y.; Wang, Y.; Capell, T.; Shi, L.; Ni, X.; Sandmann, G.; Christou, P.; Zhu, C.
Cloning and functional characterization of the maize (Zea mays L.) carotenoid epsilon hydroxylase gene
PLoS ONE
10
e0128758
2015
Zea mays (K9J9Z8), Zea mays, Zea mays L. cv B73 (K9J9Z8)
brenda
Takemura, M.; Maoka, T.; Misawa, N.
Biosynthetic routes of hydroxylated carotenoids (xanthophylls) in Marchantia polymorpha, and production of novel and rare xanthophylls through pathway engineering in Escherichia coli
Planta
241
699-710
2015
Marchantia polymorpha (A0A0E4B3I0), Marchantia polymorpha
brenda
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