BRENDA - Enzyme Database

Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin

Jönsson, T.J.; Murray, M.S.; Johnson, L.C.; Poole, L.B.; Lowther, W.T.; Biochemistry 44, 8634-8642 (2005)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
1.8.98.2
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.8.98.2
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
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.8.98.2
Homo sapiens
Q9BYN0
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.8.98.2
-
Homo sapiens
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.98.2
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
658132
Homo sapiens
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
1.8.98.2
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
the ATP molecule is cleaved between the beta- and gamma-phosphate groups
658132
Homo sapiens
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.8.98.2
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.8.98.2
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
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.8.98.2
-
Homo sapiens
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.98.2
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
658132
Homo sapiens
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
1.8.98.2
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
the ATP molecule is cleaved between the beta- and gamma-phosphate groups
658132
Homo sapiens
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?