BRENDA - Enzyme Database

Mutagenesis and modeling of the peroxiredoxin (Prx) complex with the NMR structure of ATP-bound human sulfiredoxin implicate aspartate 187 of Prx I as the catalytic residue in ATP hydrolysis

Lee, D.Y.; Park, S.J.; Jeong, W.; Sung, H.J.; Oho, T.; Wu, X.; Rhee, S.G.; Gruschus, J.M.; Biochemistry 45, 15301-15309 (2006)

Data extracted from this reference:

Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.8.98.2
14000
-
-
Homo sapiens
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.8.98.2
Homo sapiens
Q9BYN0
-
-
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
-
667711
Homo sapiens
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
r
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.8.98.2
14000
-
-
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
-
667711
Homo sapiens
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
r