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Literature summary for 1.8.98.2 extracted from

  • J๖nsson, T.J.; Murray, M.S.; Johnson, L.C.; Poole, L.B.; Lowther, W.T.
    Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin (2005), Biochemistry, 44, 8634-8642.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of the wild-type and SeMet forms of ET-hSrx were obtained by the vapor diffusion method. 1.65 A crystal structure of human Srx Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH Homo sapiens repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9BYN0
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Purification (Commentary)

Purification (Comment) Organism
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Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH the ATP molecule is cleaved between the beta- and gamma-phosphate groups Homo sapiens peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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?

Synonyms

Synonyms Comment Organism
peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase
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Homo sapiens
Srx
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Homo sapiens
sulphiredoxin
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Homo sapiens