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Literature summary for 1.23.5.1 extracted from

  • 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 (2012), Phycologia, 51, 359-370.
No PubMed abstract available

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid membrane
-
Mantoniella squamata 42651
-
thylakoid membrane
-
Spinacia oleracea 42651
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
antheraxanthin + L-ascorbate Mantoniella squamata
-
zeaxanthin + L-dehydroascorbate + H2O
-
?
antheraxanthin + L-ascorbate Spinacia oleracea
-
zeaxanthin + L-dehydroascorbate + H2O
-
?
antheraxanthin + L-ascorbate Mantoniella squamata CCAP 1965/1
-
zeaxanthin + L-dehydroascorbate + H2O
-
?
additional information Mantoniella squamata 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 Spinacia oleracea 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 Mantoniella squamata CCAP 1965/1 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 ?
-
?
violaxanthin + L-ascorbate Mantoniella squamata
-
antheraxanthin + L-dehydroascorbate + H2O
-
?
violaxanthin + L-ascorbate Spinacia oleracea
-
antheraxanthin + L-dehydroascorbate + H2O
-
?
violaxanthin + L-ascorbate Mantoniella squamata CCAP 1965/1
-
antheraxanthin + L-dehydroascorbate + H2O
-
?

Organism

Organism UniProt Comment Textmining
Mantoniella squamata
-
-
-
Mantoniella squamata CCAP 1965/1
-
-
-
Spinacia oleracea Q9SM43
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme partially by preparation of thylakoid membranes, further purifications of the VDE by, i.e. anion exchange chromatography and gel filtration, lead to a significant loss of VDE activity Mantoniella squamata

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
antheraxanthin + L-ascorbate
-
Mantoniella squamata zeaxanthin + L-dehydroascorbate + H2O
-
?
antheraxanthin + L-ascorbate
-
Spinacia oleracea zeaxanthin + L-dehydroascorbate + H2O
-
?
antheraxanthin + L-ascorbate
-
Mantoniella squamata CCAP 1965/1 zeaxanthin + L-dehydroascorbate + H2O
-
?
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 Mantoniella squamata ?
-
?
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 Spinacia oleracea ?
-
?
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 Mantoniella squamata ?
-
?
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 Mantoniella squamata CCAP 1965/1 ?
-
?
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 Mantoniella squamata CCAP 1965/1 ?
-
?
violaxanthin + L-ascorbate
-
Mantoniella squamata antheraxanthin + L-dehydroascorbate + H2O
-
?
violaxanthin + L-ascorbate
-
Spinacia oleracea antheraxanthin + L-dehydroascorbate + H2O
-
?
violaxanthin + L-ascorbate
-
Mantoniella squamata CCAP 1965/1 antheraxanthin + L-dehydroascorbate + H2O
-
?

Synonyms

Synonyms Comment Organism
VDE
-
Mantoniella squamata
VDE
-
Spinacia oleracea
Vx de-epoxidase
-
Mantoniella squamata
Vx de-epoxidase
-
Spinacia oleracea

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Mantoniella squamata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.2
-
assay at Mantoniella squamata