BRENDA - Enzyme Database

ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin

Biteau, B.; Labarre, J.; Toledano, M.B.; Nature 425, 980-984 (2003)

Data extracted from this reference:

Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.8.98.2
Mg2+
required
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.8.98.2
Saccharomyces cerevisiae
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.8.98.2
recombinant
Saccharomyces cerevisiae
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
-
659998
Saccharomyces cerevisiae
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
1.8.98.2
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
659998
Saccharomyces cerevisiae
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.8.98.2
Mg2+
required
Saccharomyces cerevisiae
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
Saccharomyces cerevisiae
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.8.98.2
recombinant
Saccharomyces cerevisiae
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
-
659998
Saccharomyces cerevisiae
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?
1.8.98.2
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
659998
Saccharomyces cerevisiae
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
?