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Literature summary for 1.11.1.24 extracted from

  • Konig, J.; Baier, M.; Horling, F.; Kahmann, U.; Harris, G.; Schurmann, P.; Dietz, K.J.
    The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux (2002), Proc. Natl. Acad. Sci. USA, 99, 5738-5743.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.24

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Hordeum vulgare 9507
-
thylakoid reversible binding of the oligomeric form of the enzyme to the thylakoid membrane Hordeum vulgare 9579
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Hordeum vulgare the midpoint redox potential of -315 mV places 2-Cys Prx reduction after Calvin cycle activation and before switching the male valve for export of excess reduction equivalents to the cytosol. The activity of the enzyme is also linked to chloroplastic NAD(P)H metabolism. Saline-stress-induced oligomerization of the enzyme triggers membrane attachment and allows for detoxification of peroxides at the site of production in immediate vicinity of the thylakoid membrane ?
-
 ?

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
 var. Gerbel
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Hordeum vulgare
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2O2 + reduced thioredoxin thioredoxin from Escherichia coli and thioredoxin f and m from spinach Hordeum vulgare H2O + oxidized thioredoxin
-
 ?
additional information the midpoint redox potential of -315 mV places 2-Cys Prx reduction after Calvin cycle activation and before switching the male valve for export of excess reduction equivalents to the cytosol. The activity of the enzyme is also linked to chloroplastic NAD(P)H metabolism. Saline-stress-induced oligomerization of the enzyme triggers membrane attachment and allows for detoxification of peroxides at the site of production in immediate vicinity of the thylakoid membrane Hordeum vulgare ?
-
 ?

Synonyms

Synonyms Comment Organism
2-Cys peroxiredoxin
-
 Hordeum vulgare
2-Cys Prx
-
 Hordeum vulgare