1.23.5.1: violaxanthin de-epoxidase
This is an abbreviated version!
For detailed information about violaxanthin de-epoxidase, go to the full flat file.
Word Map on EC 1.23.5.1
-
1.23.5.1
-
vertical
-
xanthophyll
-
zeaxanthin
-
thylakoids
-
photoelectron
-
de-epoxidation
-
photosystem
-
photoprotection
-
non-photochemical
-
adiabatic
-
antheraxanthin
-
photoinhibition
-
ccsdt
-
coupled-cluster
-
monogalactosyldiacylglycerol
-
barrier-free
-
photodetachment
-
lowest-energy
-
diadinoxanthin
-
pi-scei
-
transthylakoid
-
deepoxidase
- 1.23.5.1
-
vertical
-
xanthophyll
- zeaxanthin
- thylakoids
-
photoelectron
-
de-epoxidation
-
photosystem
-
photoprotection
-
non-photochemical
-
adiabatic
- antheraxanthin
-
photoinhibition
-
ccsdt
-
coupled-cluster
- monogalactosyldiacylglycerol
-
barrier-free
-
photodetachment
-
lowest-energy
- diadinoxanthin
-
pi-scei
-
transthylakoid
-
deepoxidase
Reaction
Synonyms
AhVDE, CsVDE, EC 1.10.99.3, lipocalin-like protein, NPQ1, VDE, Vio de-epoxidase, violaxanthin de-epoxidase, Vx de-epoxidase, ZmVDE1
ECTree
Advanced search results
General Information
General Information on EC 1.23.5.1 - violaxanthin de-epoxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
-
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
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
-
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
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
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