CATH Classification
Domain Context
CATH Clusters
| Superfamily | Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, ParB domain |
| Functional Family | Sulfiredoxin |
Enzyme Information
| 1.8.98.2 |
Sulfiredoxin.
based on mapping to UniProt Q9BYN0
Peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin- (S-hydroxycysteine) + ADP + phosphate + R-S-S-R.
-!- In the course of the reaction of EC 1.11.1.15, its cysteine residue is alternately oxidized to the sulfenic acid, S-hydroxycysteine, and reduced back to cysteine. -!- Occasionally the S-hydroxycysteine residue is further oxidized to the sulfinic acid S-hydroxy-S-oxocysteine, thereby inactivating the enzyme. -!- The reductase provides a mechanism for regenerating the active form of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form. -!- Apparently the reductase first catalyzes the phosphorylation of the -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the peroxiredoxin by a cysteine residue, forming an -S(O)-S- link between the two enzymes. -!- Attack by a thiol splits this bond, leaving the peroxiredoxin as the sulfenic acid and the reductase as the thiol.
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UniProtKB Entries (1)
| Q9BYN0 |
SRXN1_HUMAN
Homo sapiens
Sulfiredoxin-1
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PDB Structure
| PDB | 2B6F |
| External Links | |
| Method | SOLUTION NMR |
| Organism | Escherichia |
| Primary Citation |
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
Biochemistry
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