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Literature summary for 1.23.5.1 extracted from

  • Grotz, B.; Molnar, P.; Stransky, H.; Hager, A.
    Substrate specificity and functional aspects of violaxanthin-de-epoxidase, an enzyme of the xanthophyll cycle (1999), J. Plant Physiol., 154, 437-446.
No PubMed abstract available
Search for more literature for 1.23.5.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3
-
 antheraxanthin
-
 Spinacia oleracea
11.1
-
 violaxanthin
-
 Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid
-
 Spinacia oleracea 9579
-

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
antheraxanthin + ascorbate
-
 Spinacia oleracea zeaxanthin + dehydroascorbate + H2O
-
 ?
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 Spinacia oleracea ?
-
 ?
violaxanthin + ascorbate
-
 Spinacia oleracea antheraxanthin + dehydroascorbate + H2O
-
 ?