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
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1.23.5.1
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vertical
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xanthophyll
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zeaxanthin
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thylakoids
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photoelectron
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de-epoxidation
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photosystem
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photoprotection
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non-photochemical
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adiabatic
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antheraxanthin
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photoinhibition
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ccsdt
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coupled-cluster
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monogalactosyldiacylglycerol
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barrier-free
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photodetachment
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lowest-energy
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diadinoxanthin
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pi-scei
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transthylakoid
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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
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Localization
Localization on EC 1.23.5.1 - violaxanthin de-epoxidase
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additional information
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no expression in the cytoplasm or cell membrane of cucumber cotyledon protoplasts
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lumen, the soluble luminal protein VDE to attach to the thylakoid membrane
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regulation of the violaxanthin de-epoxidase involves a conformational change at low lumenal pH, followed by binding of the enzyme to the thylakoid membrane. Protonation of His at low pH induces the conformational change of the enzyme, and hence indirectly regulates binding of the enzyme to the thylakoid membrane
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the enzyme is mobile within the thylakoid lumen at neutral pH values which occur under in-vivo conditions in the dark. However, upon strong illumination, when the lumen pH drops below pH 6.5 due to formation of a proton gradient, the properties of the de-epoxidase are altered and the enzyme becomes tightly bound to the membrane thus gaining access to its substrate
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regulation of the violaxanthin de-epoxidase involves a conformational change at low lumenal pH, followed by binding of the enzyme to the thylakoid membrane. Protonation of His at low pH induces the conformational change of the enzyme, and hence indirectly regulates binding of the enzyme to the thylakoid membrane
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a water soluble lumenal enzyme, change in enzyme conformation is accompanied by the functional binding of the enzymes to the thylakoid membrane, where the substrate violaxanthin is located
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violaxanthin de-epoxidation most probably takes place inside MGDG-rich domains of the thylakoid membrane