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Literature summary for 1.14.15.21 extracted from

  • 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 (2001), Planta, 213, 446-456.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
antheraxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mantoniella squamata 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 violaxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
zeaxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mantoniella squamata
-
antheraxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?

Organism

Organism UniProt Comment Textmining
Mantoniella squamata
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
antheraxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 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 Mantoniella squamata violaxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
zeaxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mantoniella squamata antheraxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?