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all-trans-neoxanthin + ascorbate
? + dehydroascorbate + H2O
antheraxanthin + acceptor
zeaxanthin + reduced acceptor
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
cryptoxanthin epoxide + ascorbate
?
-
92% of the activity with violaxanthin
-
-
?
cryptoxanthin-5,6,5',6'-di-epoxide + ascorbate
? + dehydroascorbate + H2O
cryptoxanthin-5,6-epoxide + ascorbate
? + dehydroascorbate + H2O
diadinoxanthin + ascorbate
?
-
the activity is 2.25fold higher than the activity of violaxanthin
-
-
?
diadinoxanthin + ascorbate
? + dehydroascorbate + H2O
lutein epoxide + ascorbate
?
-
the activity is 1.33fold higher than the activity of violaxanthin
-
-
?
lutein-5,6-epoxide + ascorbate
? + dehydroascorbate + H2O
neoxanthin + ascorbate
?
-
10% of the activity with violaxanthin
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
violaxanthin + acceptor
antheraxanthin + reduced acceptor
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
additional information
?
-
all-trans-neoxanthin + ascorbate
? + dehydroascorbate + H2O
-
0.21% of the activity with violaxanthin
-
-
?
all-trans-neoxanthin + ascorbate
? + dehydroascorbate + H2O
-
2.5% of the activity with violaxanthin
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
violaxanthin de-epoxidase and zeaxanthin epoxidase catalyze the addition and removal of epoxide groups in carotenoids of xanthophyll cycle in plants. The xanthophyll cycle is implicated in protecting the photosynthetoic apparatus from excessive light
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
the activity is 5.25fold higher than the activity of violaxanthin
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
the violaxanthin/antheraxanthin cycle in Mantionella is caused by the interaction of the slow second de-epoxidation step and the relatively fast epoxidation of antheraxanthin to violaxanthin
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
11% of the activity with violaxanthin
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
violaxanthin de-epoxidase and zeaxanthin epoxidase catalyze the addition and removal of epoxide groups in carotenoids of xanthophyll cycle in plants. The xanthophyll cycle is implicated in protecting the photosynthetoic apparatus from excessive light
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of the chloroplast against photooxidative damage. Violaxanthin is bound to the antenna proteins of both photosystems. In photosystem II, the formation of zeaxanthin is essential for the pH-dependent dissipation of excess light energy as heat. Violaxanthin bound to site V1 and N1 is easily accessible for de-epoxidation, whereas violaxanthin bound to L2 is only partially and/or with the slower kinetics converible to zeaxanthin
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
146% of the activity with violaxanthin
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
reaction of the xanthophyll cycle
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
cryptoxanthin-5,6,5',6'-di-epoxide + ascorbate
? + dehydroascorbate + H2O
-
36.5% of the activity with violaxanthin
-
-
?
cryptoxanthin-5,6,5',6'-di-epoxide + ascorbate
? + dehydroascorbate + H2O
-
54% of the activity with violaxanthin
-
-
?
cryptoxanthin-5,6-epoxide + ascorbate
? + dehydroascorbate + H2O
-
1% of the activity with violaxanthin
-
-
?
cryptoxanthin-5,6-epoxide + ascorbate
? + dehydroascorbate + H2O
-
12.5% of the activity with violaxanthin
-
-
?
diadinoxanthin + ascorbate
? + dehydroascorbate + H2O
-
11% of the activity with violaxanthin
-
-
?
diadinoxanthin + ascorbate
? + dehydroascorbate + H2O
-
69% of the activity with violaxanthin
-
-
?
lutein-5,6-epoxide + ascorbate
? + dehydroascorbate + H2O
-
20% of the activity with violaxanthin
-
-
?
lutein-5,6-epoxide + ascorbate
? + dehydroascorbate + H2O
-
110% of the activity with violaxanthin
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
-
-
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
overall reaction
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
overall reaction
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
overall reaction
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
overall reaction
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
violaxanthin de-epoxidase and zeaxanthin epoxidase catalyze the addition and removal of epoxide groups in carotenoids of xanthophyll cycle in plants. The xanthophyll cycle is implicated in protecting the photosynthetic apparatus from excessive light
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
violaxanthin de-epoxidase and zeaxanthin epoxidase catalyze the addition and removal of epoxide groups in carotenoids of xanthophyll cycle in plants. The xanthophyll cycle is implicated in protecting the photosynthetic apparatus from excessive light
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of the chloroplast against photooxidative damage. Violaxanthin is bound to the antenna proteins of both photosystems. In photosystem II, the formation of zeaxanthin is essential for the pH-dependent dissipation of excess light energy as heat. Violaxanthin bound to site V1 and N1 is easily accessible for de-epoxidation, whereas violaxanthin bound to L2 is only partially and/or with the slower kinetics converible to zeaxanthin
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
reaction of the xanthophyll cycle
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
additional information
?
-
-
VDE is the first described putative plant lipocalin
-
-
?
additional information
?
-
-
the enzyme is inactive against monoepoxy and diepoxy beta-carotene, antheraxanthin-A and lutein epoxide
-
-
?
additional information
?
-
-
no activity with 9-cis neoxanthin and 9-cis violaxanthin
-
-
?
additional information
?
-
-
high concentrations of available violaxanthin, as found in enzyme assays with pure violaxanthin, lead to saturation of the VDE and a strong competition with the intermediate reaction product Ax, thus decreasing the ratio of the second deepoxidation rate to the first de-epoxidation rate
-
-
?
additional information
?
-
-
Mantoniella squamata VDE exhibits a very low ratio of the second de-epoxidation rate to the first de-epoxidation rate in thylakoids or in enzyme assays with thte purified light-harvesting complex. The interaction between the isolated light-harvesting complex and the VDE can influence the ratio of the two de-epoxidation rates. Mantoniella squamata VDE is able to de-epoxidize violaxanthin bound to spinach light harvesting complex II better than bound to Mantoniella squamata light harvesting complex II, the latter shows accumulation of intermediate antheraxanthin in the membranes, rate constants for first and second reaction step, overview
-
-
?
additional information
?
-
-
high concentrations of available violaxanthin, as found in enzyme assays with pure violaxanthin, lead to saturation of the VDE and a strong competition with the intermediate reaction product Ax, thus decreasing the ratio of the second deepoxidation rate to the first de-epoxidation rate
-
-
?
additional information
?
-
-
Mantoniella squamata VDE exhibits a very low ratio of the second de-epoxidation rate to the first de-epoxidation rate in thylakoids or in enzyme assays with thte purified light-harvesting complex. The interaction between the isolated light-harvesting complex and the VDE can influence the ratio of the two de-epoxidation rates. Mantoniella squamata VDE is able to de-epoxidize violaxanthin bound to spinach light harvesting complex II better than bound to Mantoniella squamata light harvesting complex II, the latter shows accumulation of intermediate antheraxanthin in the membranes, rate constants for first and second reaction step, overview
-
-
?
additional information
?
-
-
the level of violaxanthin de-epoxidase changes in an inverse, nonlinear relationship with respect to the VAZ pool (violaxanthin + antheraxanthin + zeaxanthin), suggesting that enzyme levels can be indirectly regulated by the VAZ pool
-
-
?
additional information
?
-
-
no activity with 9-cis neoxanthin and 9-cis violaxanthin
-
-
?
additional information
?
-
-
only the epoxy-oxygen at the 5,6(5',6') position of xanthophylls are cleaved by the VDE, whereas ring-spanning epoxides at position 3,6(3',6') are not accessible to the enzyme. The structure and chemical ligands of the second jonon ring are insignificant for the de-epoxidation of the 5,6-epoxy groups of the first ring. The epoxy-free second jonon ring is not involved in the binding of the xanthophyll to the catalytic center and does not affect the enzyme reaction. Due to steric hindrance, any tested cis-configuration in the polyene chain of the xanthophylls, as well as the 8-oxy group, in fucoxanthin, prevents the de-epoxidation
-
-
?
additional information
?
-
spinach VDE is able to de-epoxidize violaxanthin bound to spinach or Mantoniella squamata light harvesting complexes in a comparable manner, rate constants for first and second reaction step, overview
-
-
?
additional information
?
-
by measuring the initial formation of the product, enzyme VDE is found to convert a large number of violaxanthin molecules to antheraxanthin before producing any zeaxanthin, favoring a model where violaxanthin is bound non-symmetrically in VDE, overview
-
-
?
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antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
additional information
?
-
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
violaxanthin de-epoxidase and zeaxanthin epoxidase catalyze the addition and removal of epoxide groups in carotenoids of xanthophyll cycle in plants. The xanthophyll cycle is implicated in protecting the photosynthetoic apparatus from excessive light
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
the violaxanthin/antheraxanthin cycle in Mantionella is caused by the interaction of the slow second de-epoxidation step and the relatively fast epoxidation of antheraxanthin to violaxanthin
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
violaxanthin de-epoxidase and zeaxanthin epoxidase catalyze the addition and removal of epoxide groups in carotenoids of xanthophyll cycle in plants. The xanthophyll cycle is implicated in protecting the photosynthetoic apparatus from excessive light
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of the chloroplast against photooxidative damage. Violaxanthin is bound to the antenna proteins of both photosystems. In photosystem II, the formation of zeaxanthin is essential for the pH-dependent dissipation of excess light energy as heat. Violaxanthin bound to site V1 and N1 is easily accessible for de-epoxidation, whereas violaxanthin bound to L2 is only partially and/or with the slower kinetics converible to zeaxanthin
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + ascorbate
zeaxanthin + dehydroascorbate + H2O
-
reaction of the xanthophyll cycle
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
?
antheraxanthin + L-ascorbate
zeaxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
-
-
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
overall reaction
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
overall reaction
-
-
?
violaxanthin + 2 L-ascorbate
zeaxanthin + 2 L-dehydroascorbate + 2 H2O
overall reaction
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
violaxanthin de-epoxidase and zeaxanthin epoxidase catalyze the addition and removal of epoxide groups in carotenoids of xanthophyll cycle in plants. The xanthophyll cycle is implicated in protecting the photosynthetic apparatus from excessive light
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
violaxanthin de-epoxidase and zeaxanthin epoxidase catalyze the addition and removal of epoxide groups in carotenoids of xanthophyll cycle in plants. The xanthophyll cycle is implicated in protecting the photosynthetic apparatus from excessive light
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of the chloroplast against photooxidative damage. Violaxanthin is bound to the antenna proteins of both photosystems. In photosystem II, the formation of zeaxanthin is essential for the pH-dependent dissipation of excess light energy as heat. Violaxanthin bound to site V1 and N1 is easily accessible for de-epoxidation, whereas violaxanthin bound to L2 is only partially and/or with the slower kinetics converible to zeaxanthin
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + ascorbate
antheraxanthin + dehydroascorbate + H2O
-
reaction of the xanthophyll cycle
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
?
violaxanthin + L-ascorbate
antheraxanthin + L-dehydroascorbate + H2O
-
-
-
-
?
additional information
?
-
-
VDE is the first described putative plant lipocalin
-
-
?
additional information
?
-
-
high concentrations of available violaxanthin, as found in enzyme assays with pure violaxanthin, lead to saturation of the VDE and a strong competition with the intermediate reaction product Ax, thus decreasing the ratio of the second deepoxidation rate to the first de-epoxidation rate
-
-
?
additional information
?
-
-
high concentrations of available violaxanthin, as found in enzyme assays with pure violaxanthin, lead to saturation of the VDE and a strong competition with the intermediate reaction product Ax, thus decreasing the ratio of the second deepoxidation rate to the first de-epoxidation rate
-
-
?
additional information
?
-
-
the level of violaxanthin de-epoxidase changes in an inverse, nonlinear relationship with respect to the VAZ pool (violaxanthin + antheraxanthin + zeaxanthin), suggesting that enzyme levels can be indirectly regulated by the VAZ pool
-
-
?
additional information
?
-
spinach VDE is able to de-epoxidize violaxanthin bound to spinach or Mantoniella squamata light harvesting complexes in a comparable manner, rate constants for first and second reaction step, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
-
the four putative activation residues D98, D117, H168 and D206 play are all conserved in plants but not in diatoms
evolution
-
the violaxanthin cycle: under strong light conditions, enzyme violaxanthin de-epoxidase catalyses de-epoxidation of violaxanthin (Vx) to zeaxanthin via antheraxanthin as an intermediate product. This type of the cycle exists in higher plants, ferns, mosses and some group of algae
evolution
nucleotide diversity analysis of VDE1 in maize and teosinte indicates that its exon has less genetic variation, consistent with the conserved function of VDE1 in plants. In addition, dramatically reduced nucleotide diversity, fewer haplotypes and a significantly negative parameter deviation for Tajima's D test of ZmVDE1 in maize and teosinte suggest that a potential selective force has acted across the ZmVDE1 locus. A 4.2 Mb selective sweep with low recombination surrounding the ZmVDE1 locus has resulted in severely reduced nucleotide diversity on chromosome 2. Natural selection and the conserved domains of ZmVDE1 might show an important role in the xanthophyll cycle of the carotenoid biosynthesis pathway. Maize domestication involves a radical phenotypic transformation, resulting in an unbranched plant with numerous exposed seed attached to a cob in 20 rows or more. The dramatic morphological changes from teosinte to maize likely involved alterations in only a few significant genes with large effect. Evolution of the ZmVDE1 locus in maize and teosinte, overview
evolution
-
nucleotide diversity analysis of VDE1 in maize and teosinte indicates that its exon has less genetic variation, consistent with the conserved function of VDE1 in plants. In addition, dramatically reduced nucleotide diversity, fewer haplotypes and a significantly negative parameter deviation for Tajima's D test of ZmVDE1 in maize and teosinte suggest that a potential selective force has acted across the ZmVDE1 locus. A 4.2 Mb selective sweep with low recombination surrounding the ZmVDE1 locus has resulted in severely reduced nucleotide diversity on chromosome 2. Natural selection and the conserved domains of ZmVDE1 might show an important role in the xanthophyll cycle of the carotenoid biosynthesis pathway. Maize domestication involves a radical phenotypic transformation, resulting in an unbranched plant with numerous exposed seed attached to a cob in 20 rows or more. The dramatic morphological changes from teosinte to maize likely involved alterations in only a few significant genes with large effect. Evolution of the ZmVDE1 locus in maize and teosinte, overview
malfunction
a reduction in enzyme expression results in greater photosensitivity
malfunction
mutational reduction of the disulfides in the enzyme results in loss of a rigid structure and a decrease in thermal stability of 15°C
metabolism
-
the xanthophyll cycle is an important photoprotective process functioning in plants. One of its forms, the violaxanthin cycle, involves interconversion between violaxanthin, antheraxanthin, and zeaxanthin
metabolism
natural selection and the conserved domains of ZmVDE1 might show an important role in the xanthophyll cycle of the carotenoid biosynthesis pathway
metabolism
-
natural selection and the conserved domains of ZmVDE1 might show an important role in the xanthophyll cycle of the carotenoid biosynthesis pathway
physiological function
the expression of the violaxanthin de-epoxidase gene in transgenic plants affects the sensitivity of photosystem II photoinhibition to high light and chilling stress
physiological function
-
the carotenoid zeaxanthin, synthesized from violaxanthin by violaxanthin de-epoxidase plays a major role in the protection from excess illumination
physiological function
-
VDE is a water soluble lumenal protein that undergoes a conformational change when pH drops due to formation of the light-driven proton gradient across the thylakoid membrane. The change in enzyme conformation is accompanied by the functional binding of the enzymes to the thylakoid membrane, where the substrate violaxanthin is located
physiological function
-
violaxanthin de-epoxidase plays an important role in protecting the photosynthetic apparatus from photo-damage by dissipating excessively absorbed light energy as heat, via the conversion of violaxanthin (V) to intermediate product antheraxanthin and final product zeaxanthin under high light stress
physiological function
the endogenous level of the enzyme is rate-limiting for non-photochemical quenching in Arabidopsis under subsaturating but not saturating light and can become rate-limiting under chilling conditions
physiological function
translation initiation factor eIFiso4G expression is required to regulate violaxanthin de-epoxidase expression and to support photosynthetic activity. An increase in the transcript and protein levels of violaxanthin de-epoxidase in the eIFiso4G loss of function mutant and an increase in its xanthophyll de-epoxidation state correlate with the higher quenching through dissipation as heat associated with loss of eIFiso4G expression
physiological function
photosynthetic organisms need protection against excessive light. By using non-photochemical quenching, where the excess light is converted into heat, the organism can survive at higher light intensities. This process is partly initiated by the formation of zeaxanthin, which is achieved by the de-epoxidation of violaxanthin and antheraxanthin to zeaxanthin. This reaction is catalyzed by violaxanthin de-epoxidase (VDE)
physiological function
role of peanut VDE increasing the xanthophyll cycle and the de-epoxidation state, overview. Overexpressing AhVDE protect membrane from damage under stress alleviating the damage of peroxidation and RNAi aggregated by such damage
physiological function
violaxanthin de-epoxidase (VDE) catalyses the conversion of violaxanthin to zeaxanthin at the lumen side of the thylakoids during exposure to intense light
physiological function
violaxanthin de-epoxidase (VDE) has a critical role in the carotenoid biosynthesis pathway, which is involved in protecting the photosynthesis apparatus from damage caused by excessive light. The enzyme functions as an important synthetase involved in nutrient accumulation in maize kernels. VDE has a conserved function in plants
physiological function
-
violaxanthin de-epoxidase (VDE) has a critical role in the carotenoid biosynthesis pathway, which is involved in protecting the photosynthesis apparatus from damage caused by excessive light. VDE has a conserved function in plants
physiological function
violaxanthin to zeaxanthin conversion is catalyzed by the lumenal enzyme violaxanthin de-epoxidase (VDE), using ascorbate as reducing power. Enzyme VDE is activated by a decrease of pH in the lumen, occurring when light driven proton translocation across the thylakoids membrane exceeds ATPase activity. The redox potential has a major influence on enzyme VDE activity, overview
additional information
-
molecular dynamics and simulations, overview
additional information
enzyme VDE is active in its completely oxidized form presenting six disulfide bonds. Redox titration show that VDE activity is sensitive to variation in redox potential, suggesting the possibility that dithiol/disulfide exchange reactions may represent a mechanism for VDE regulation
additional information
-
enzyme VDE is active in its completely oxidized form presenting six disulfide bonds. Redox titration show that VDE activity is sensitive to variation in redox potential, suggesting the possibility that dithiol/disulfide exchange reactions may represent a mechanism for VDE regulation
additional information
VDE enzyme activity is possible without the C-terminal domain but not without the N-terminal domain. The N-terminal domain shows no VDE activity by itself, but when separately expressed domains are mixed, VDE activity is possible
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C118A
site-directed mutagenesis, inactive mutant
C14A
site-directed mutagenesis, inactive mutant
C21A
site-directed mutagenesis, almost inactive mutant
C249A
site-directed mutagenesis, inactive mutant
C27A
site-directed mutagenesis, inactive mutant
C33A
site-directed mutagenesis, inactive mutant
C37A
site-directed mutagenesis, inactive mutant
C46A
site-directed mutagenesis, inactive mutant
C50A
site-directed mutagenesis, the mutant shows 96.5% reduced activity compared to the wild-type enzyme
C65A
site-directed mutagenesis, the mutant shows 95.3% reduced activity compared to the wild-type enzyme
C72A
site-directed mutagenesis, almost inactive mutant
C7A
site-directed mutagenesis, the mutant shows 14.8% reduced activity compared to the wild-type enzyme
C9A
site-directed mutagenesis, inactive mutant
D178A
the mutant shows 56% activity compared to the wild type enzyme
DELTA1-4
-
removal of 4 amino acids from the N-terminal region abolishes all violaxanthin de-epoxidase activity
DELTA258-349
-
71 C-terminal amino acid can be removed without affecting activity
F123A
the mutant shows 34% activity compared to the wild type enzyme
F155A
the mutant shows 5% activity compared to the wild type enzyme
H121A
the mutant shows 5% activity compared to the wild type enzyme
N167A
the mutant shows 121% activity compared to the wild type enzyme
Q119A
the mutant shows 32% activity compared to the wild type enzyme
Q153A
the mutant shows 75% activity compared to the wild type enzyme
Q153E
the mutant shows 60% activity compared to the wild type enzyme
Q153L
the mutant shows 30% activity compared to the wild type enzyme
T245A
the mutant shows 82% activity compared to the wild type enzyme
W179A
the mutant shows less than 2% activity compared to the wild type enzyme
W179N
the mutant shows less than 2% activity compared to the wild type enzyme
Y175F
the mutant shows 62% activity compared to the wild type enzyme
Y214F
the mutant shows less than 2% activity compared to the wild type enzyme
C09S
site-directed mutagenesisthe mutant shows slightly decreased activity compared to the wild-type enzyme
C118S
site-directed mutagenesis, almost inactive mutant
C14S
site-directed mutagenesis, almost inactive mutant
C21S
site-directed mutagenesis, almost inactive mutant
C248S
site-directed mutagenesis, the mutant shows over 95% reduced activity compared to the wild-type enzyme
C27S
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
C33S
site-directed mutagenesis, the mutant shows about 90% reduced activity compared to the wild-type enzyme
C37S
site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
C46S
site-directed mutagenesis, the mutant shows about 45% reduced activity compared to the wild-type enzyme
C50S
site-directed mutagenesis, the mutant shows 90% reduced activity compared to the wild-type enzyme
C65S
site-directed mutagenesis, the mutant shows 85% reduced activity compared to the wild-type enzyme
C72S
site-directed mutagenesis, the mutant shows over 95% reduced activity compared to the wild-type enzyme
C7S
site-directed mutagenesis, the mutant shows 2fold increased activity compared to the wild-type enzyme
H121A/H124A
-
considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7. Km-value for ascorbate is 3.2 mM compared to 1.9 mM for wild-type enzyme
H121R/H124R
inactive mutant enzyme
H134A
-
considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7
H167A/H173A
-
considerably lower pH dependence for binding than wild-type, cooperativity value of 1.6 compared to wild-type value of 3.7. Km-value for ascorbate is 8.3 mM compared to 1.9 mM for wild-type enzyme
H167R/H173R
-
considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7. Km-value for ascorbate is 6.3 mM compared to 1.9 mM for wild-type enzyme
V65I
naturally occuring mutation with no change in charge or hydrophobicity
D117A
-
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
D117A
-
the mutant shows 40% of wild type activity
D206I
-
site-directed mutagenesis, the mutant shows 56% reduced activity compared to the wild-type enzyme
D206I
-
the mutant shows 44% of wild type activity
D86A
-
site-directed mutagenesis, the mutant shows 19% reduced activity compared to the wild-type enzyme
D86A
-
the mutant shows 86% of wild type activity
D98L
-
site-directed mutagenesis, the mutant shows 41% reduced activity compared to the wild-type enzyme
D98L
-
the mutant shows 59% of wild type activity
D98L/D117A
-
site-directed mutagenesis, the mutant shows 59% reduced activity compared to the wild-type enzyme
D98L/D117A
-
the mutant shows 41% of wild type activity
D98L/D117A/D206I
-
site-directed mutagenesis, the mutant shows 84% reduced activity compared to the wild-type enzyme
D98L/D117A/D206I
-
the mutant shows 16% of wild type activity
D98L/D117A/D206I/H168A
-
the mutant shows 6% of wild type activity
D98L/D117A/D206I/H168A
-
site-directed mutagenesis, the mutant shows 94% reduced activity compared to the wild-type enzyme
H168A
-
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme
H168A
-
the mutant shows 20% of wild type activity
H124R
-
considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7. Km-value for ascorbate is 2.1 mM compared to 1.9 mM for wild-type enzyme
H124R
-
considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7.Km-value for ascorbate is 1.5 mM compared to 1.9 mM for wild-type enzyme
additional information
the sense peanut AhVDE and Nicotiana tabacum cv. NC89 RNAi-NtVDE are introduced into tobacco plants
additional information
-
the sense peanut AhVDE and Nicotiana tabacum cv. NC89 RNAi-NtVDE are introduced into tobacco plants
additional information
-
enzyme downregulation by anti-sense expression of CsVDE in Arabidopsis thaliana showing reduced enzyme activity under high light stress
additional information
quantitative assay of 5' deletions of the CsVDE promoter in transgenic Arabidopsis thaliana
additional information
-
quantitative assay of 5' deletions of the CsVDE promoter in transgenic Arabidopsis thaliana
additional information
the C-terminally truncated VDE does not show such an oligomerization, is relatively more active at higher pH, but does not alter the KM for ascorbate
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Yamamoto, H.Y.; Higashi, R.M.
Violaxanthin de-epoxidase. Lipid composition and substrate specificity
Arch. Biochem. Biophys.
190
514-522
1978
Lactuca sativa
brenda
Latowski, D.; Kostecka, A.; Strzalka, K.
Effect of monogalactosyldiacylglycerol and other thylakoid lipids on violaxanthin de-epoxidation in liposomes
Biochem. Soc. Trans.
28
810-812
2000
Triticum aestivum
brenda
Latowski, D.; Akerlund, H.E.; Strzalka, K.
Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity
Biochemistry
43
4417-4420
2004
Triticum aestivum
brenda
Kawano, M.; Kuwabara, T.
pH-dependent reversible inhibition of violaxanthin de-epoxidase by pepstatin related to protonation-induced structural change of the enzyme
FEBS Lett.
481
101-104
2000
Spinacia oleracea
brenda
Bugos, R.C.; Hieber, A.D.; Yamamoto, H.Y.
Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants
J. Biol. Chem.
273
15321-15324
1998
Arabidopsis thaliana (Q39249), Nicotiana tabacum (Q40593), Nicotiana tabacum
brenda
Wehner, A.; Storf, S.; Jahns, P.; Schmid, V.H.
De-epoxidation of violaxanthin in light-harvesting complex I proteins
J. Biol. Chem.
279
26823-26829
2004
Solanum lycopersicum
brenda
Grotz, B.; Molnar, P.; Stransky, H.; Hager, A.
Substrate specificity and functional aspects of violaxanthin-de-epoxidase, an enzyme of the xanthophyll cycle
J. Plant Physiol.
154
437-446
1999
Spinacia oleracea
-
brenda
Arvidsson, P.O.; Eva Bratt, C.; Carlsson, M.; Aakerlund, H.E.
Purification and identification of the violaxanthin deepoxidase as a 43 kDa protein
Photosynth. Res.
49
119-129
1996
Spinacia oleracea
brenda
Emanuelsson, A.; Eskling, M.; Akerlund, H.E.
Chemical and mutational modification of histidines in violaxanthin de-epoxidase from Spinacia oleracea
Physiol. Plant.
119
97-104
2003
Spinacia oleracea (Q9SM43)
-
brenda
Gisselsson, A.; Szilagyi, A.; Akerlund, H.E.
Role of histidines in the binding of violaxanthin de-epoxidase to the thylakoid membrane as studied by site-directed mutagenesis
Physiol. Plant.
122
337-343
2004
Spinacia oleracea, Triticum aestivum
-
brenda
Kuwabara, T.; Hasegawa, M.; Kawano, M.; Takaichi, S.
Characterization of violaxanthin de-epoxidase purified in the presence of Tween 20: effects of dithiothreitol and pepstatin A
Plant Cell Physiol.
40
1119-1126
1999
Spinacia oleracea
brenda
Rockholm, D.C.; Yamamoto, H.Y.
Violaxanthin de-epoxidase
Plant Physiol.
110
697-703
1996
Lactuca sativa
brenda
Bugos, R.C.; Chang, S.H.; Yamamoto, H.Y.
Developmental expression of violaxanthin de-epoxidase in leaves of tobacco growing under high and low light
Plant Physiol.
121
207-214
1999
Nicotiana tabacum
brenda
Havir, E.A.; Tausta, S.L.; Peterson, R.B.
Purification and properties of violaxanthin de-epoxidase from spinach
Plant Sci.
123
57-66
1997
Spinacia oleracea
-
brenda
Hager, A.; Holocher, K.
Localization of the xanthophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease
Planta
192
581-589
1994
Spinacia oleracea
-
brenda
Jahns, P.; Heyde, S.
Dicyclohexylcarbodiimide alters the pH dependence of violaxanthin de-epoxidation
Planta
207
393-400
1999
Pisum sativum
-
brenda
Frommolt, R.; Goss, R.; Wilhelm, C.
The de-epoxidase and epoxidase reactions of Mantoniella squamata (Prasinophyceae) exhibit different substrate-specific reaction kinetics compared to spinach
Planta
213
446-456
2001
Spinacia oleracea, Mantoniella squamata
brenda
Hieber, A.D.; Bugos, R.C.; Verhoeven, A.S.; Yamamoto, H.Y.
Overexpression of violaxanthin de-epoxidase: properties of C-terminal deletions on activity and pH-dependent lipid binding
Planta
214
476-483
2002
Arabidopsis thaliana
brenda
Goss, R.
Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae)
Planta
217
801-812
2003
Mantoniella squamata, Spinacia oleracea
brenda
Goss, R.; Lohr, M.; Latowski, D.; Grzyb, J.; Vieler, A.; Wilhelm, C.; Strzalka, K.
Role of hexagonal structure-forming lipids in diadinoxanthin and violaxanthin solubilization and de-epoxidation
Biochemistry
44
4028-4036
2005
Triticum aestivum
brenda
Latowski, D.; Kruk, J.; Strzaska, K.
Inhibition of zeaxanthin epoxidase activity by cadmium ions in higher plants
J. Inorg. Biochem.
99
2081-2087
2005
Lemna trisulca, Solanum lycopersicum, Prunus armeniaca
brenda
Latowski, D.; Banas, A.K.; Strzaska, K.; Gabrys, H.
Amino sugars - new inhibitors of zeaxanthin epoxidase, a violaxanthin cycle enzyme
J. Plant Physiol.
164
231-237
2007
Lemna trisulca
brenda
Grouneva, I.; Jakob, T.; Wilhelm, C.; Goss, R.
Influence of ascorbate and pH on the activity of the diatom xanthophyll cycle-enzyme diadinoxanthin de-epoxidase
Physiol. Plant.
126
205-211
2006
Spinacia oleracea
brenda
Yamamoto, H.Y.
Functional roles of the major chloroplast lipids in the violaxanthin cycle
Planta
224
719-724
2006
Arabidopsis thaliana
brenda
Vieler, A.; Scheidt, H.A.; Schmidt, P.; Montag, C.; Nowoisky, J.F.; Lohr, M.; Wilhelm, C.; Huster, D.; Goss, R.
The influence of phase transitions in phosphatidylethanolamine models on the activity of violaxanthin de-epoxidase
Biochim. Biophys. Acta
1778
1027-1034
2008
Spinacia oleracea
brenda
Latwoski, D.; Goss, R.; Grzyb, J.; Akerlund, H.; Burda, K.; Kruk, J.; Strzalka, K.
De-epoxidases of xanthophyll cycles require non-bilayer lipids for their activity
Biologija (Vilnius)
53
16-20
2007
Spinacia oleracea
-
brenda
Fernandez-Marin, B.; Balaguer, L.; Esteban, R.; Becerril, J.M.; Garcia-Plazaola, J.I.
Dark induction of the photoprotective xanthophyll cycle in response to dehydration
J. Plant Physiol.
166
1734-1744
2009
Asplenium ceterach
brenda
Han, H.; Gao, S.; Li, B.; Dong, X.C.; Feng, H.L.; Meng, Q.W.
Overexpression of violaxanthin de-epoxidase gene alleviates photoinhibition of PSII and PSI in tomato during high light and chilling stress
J. Plant Physiol.
167
176-183
2009
Solanum lycopersicum (C0KZ34), Solanum lycopersicum
brenda
Goss, R.; Opitz, C.; Lepetit, B.; Wilhelm, C.
The synthesis of NPQ-effective zeaxanthin depends on the presence of a transmembrane proton gradient and a slightly basic stromal side of the thylakoid membrane
Planta
228
999-1009
2008
Spinacia oleracea
brenda
Coesel, S.; Obornik, M.; Varela, J.; Falciatore, A.; Bowler, C.
Evolutionary origins and functions of the carotenoid biosynthetic pathway in marine diatoms
PLoS ONE
3
e2896
2008
Phaeodactylum tricornutum, Thalassiosira pseudonana
brenda
Vaz, J.; Sharma, P.
Photoinhibition and photosynthetic acclimation of rice (Oryza sativa L. cv Jyothi) plants grown under different light intensities and photoinhibited under field conditions
Indian J. Biochem. Biophys.
46
253-260
2009
Oryza sativa
-
brenda
Saga, G.; Giorgetti, A.; Fufezan, C.; Giacometti, G.M.; Bassi, R.; Morosinotto, T.
Mutation analysis of violaxanthin de-epoxidase identifies substrate-binding sites and residues involved in catalysis
J. Biol. Chem.
285
23763-23770
2010
Arabidopsis thaliana (Q39249)
brenda
Gao, S.; Han, H.; Feng, H.L.; Zhao, S.J.; Meng, Q.W.
Overexpression and suppression of violaxanthin de-epoxidase affects the sensitivity of photosystem II photoinhibition to high light and chilling stress in transgenic tobacco
J. Integr. Plant Biol.
52
332-339
2010
Solanum lycopersicum (C0KZ34), Solanum lycopersicum
brenda
Latowski, D.; Goss, R.; Bojko, M.; Strzałka, K.
Violaxanthin and diadinoxanthin de-epoxidation in various model lipid systems
Acta Biochim. Pol.
59
101-103
2012
Triticum aestivum
brenda
Schaller, S.; Latowski, D.; Jemiola-Rzeminska, M.; Quaas, T.; Wilhelm, C.; Strzalka, K.; Goss, R.
The investigation of violaxanthin de-epoxidation in the primitive green alga Mantoniella squamata (Prasinophyceae) indicates mechanistic differences in xanthophyll conversion to higher plants
Phycologia
51
359-370
2012
Mantoniella squamata, Spinacia oleracea (Q9SM43), Mantoniella squamata CCAP 1965/1
-
brenda
Fufezan, C.; Simionato, D.; Morosinotto, T.
Identification of key residues for pH dependent activation of violaxanthin de-epoxidase from Arabidopsis thaliana
PLoS ONE
7
e35669
2012
Arabidopsis thaliana
brenda
Li, X.; Zhao, W.; Sun, X.; Huang, H.; Kong, L.; Niu, D.; Sui, X.; Zhang, Z.
Molecular cloning and characterization of violaxanthin de-epoxidase (CsVDE) in cucumber
PLoS ONE
8
e64383
2013
Cucumis sativus
brenda
Chen, Z.; Gallie, D.R.
Violaxanthin de-epoxidase is rate-limiting for non-photochemical quenching under subsaturating light or during chilling in Arabidopsis
Plant Physiol. Biochem.
58
66-82
2012
Arabidopsis thaliana (Q39249)
brenda
Chen, Z.; Jolley, B.; Caldwell, C.; Gallie, D.R.
Eukaryotic translation initiation factor eIFiso4G is required to regulate violaxanthin de-epoxidase expression in Arabidopsis
J. Biol. Chem.
289
13926-13936
2014
Arabidopsis thaliana (Q39249)
brenda
Gao, Z.; Liu, Q.; Zheng, B.; Chen, Y.
Molecular characterization and primary functional analysis of PeVDE, a violaxanthin de-epoxidase gene from bamboo (Phyllostachys edulis)
Plant Cell Rep.
32
1381-1391
2013
Phyllostachys edulis (R9QL67)
brenda
Simionato, D.; Basso, S.; Zaffagnini, M.; Lana, T.; Marzotto, F.; Trost, P.; Morosinotto, T.
Protein redox regulation in the thylakoid lumen the importance of disulfide bonds for violaxanthin de-epoxidase
FEBS Lett.
589
919-923
2015
Arabidopsis thaliana (Q39249), Arabidopsis thaliana
brenda
Xu, J.; Li, Z.; Yang, H.; Yang, X.; Chen, C.; Li, H.
Genetic diversity and molecular evolution of a violaxanthin de-epoxidase gene in maize
Front. Genet.
7
131
2016
Zea mays subsp. parviglumis, Zea mays subsp. mays (B6SUQ7)
brenda
Li, X.; Sui, X.; Zhao, W.; Huang, H.; Chen, Y.; Zhang, Z.
Characterization of cucumber violaxanthin de-epoxidase gene promoter in Arabidopsis
J. Biosci. Bioeng.
119
470-477
2015
Cucumis sativus (E5FPU5), Cucumis sativus
brenda
Hallin, E.I.; Guo, K.; Akerlund, H.E.
Violaxanthin de-epoxidase disulphides and their role in activity and thermal stability
Photosynth. Res.
124
191-198
2015
Spinacia oleracea (Q9SM43), Spinacia oleracea
brenda
Hallin, E.I.; Guo, K.; Akerlund, H.E.
Functional and structural characterization of domain truncated violaxanthin de-epoxidase
Physiol. Plant.
157
414-421
2016
Spinacia oleracea (Q9SM43)
brenda
Yang, S.; Meng, D.Y.; Hou, L.L.; Li, Y.; Guo, F.; Meng, J.J.; Wan, S.B.; Li, X.G.
Peanut violaxanthin de-epoxidase alleviates the sensitivity of PSII photoinhibition to heat and high irradiance stress in transgenic tobacco
Plant Cell Rep.
34
1417-1428
2015
Arachis hypogaea (L0HNF3), Arachis hypogaea
brenda