KEGG   ENZYME: 1.8.98.2Help
Entry
EC 1.8.98.2                 Enzyme                                 

Name
sulfiredoxin;
Srx1;
sulphiredoxin;
peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With other, known, acceptors
BRITE hierarchy
Sysname
peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]
Reaction(IUBMB)
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
Substrate
peroxiredoxin-(S-hydroxy-S-oxocysteine);
ATP [CPD:C00002];
RSH [CPD:C01336]
Product
peroxiredoxin-(S-hydroxycysteine);
ADP [CPD:C00008];
phosphate [CPD:C00009];
R-S-S-R
Comment
In the course of the reaction of EC 1.11.1.15, peroxiredoxin, 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 catalyses 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.
History
EC 1.8.98.2 created 2005
Orthology
K12260  
sulfiredoxin
Genes
HSA: 
140809(SRXN1)
PTR: 
469853(SRXN1)
PPS: 
100983325(SRXN1)
GGO: 
101149749(SRXN1)
PON: 
100437984(SRXN1)
NLE: 
100601542(SRXN1)
MCC: 
714997(SRXN1)
MCF: 
102125068(SRXN1)
CJC: 
100386992(SRXN1)
MMU: 
76650(Srxn1)
RNO: 
296271(Srxn1)
CGE: 
100759653(Srxn1)
NGI: 
103751626(Srxn1)
HGL: 
101726463(Srxn1)
OCU: 
100359116(SRXN1)
TUP: 
CFA: 
100686728(SRXN1)
AML: 
UMR: 
103674490(SRXN1)
FCA: 
101090507(SRXN1)
PTG: 
102956412(SRXN1)
BTA: 
531606(SRXN1)
BOM: 
102264913(SRXN1)
PHD: 
102334004(SRXN1)
CHX: 
OAS: 
101121699(SRXN1)
SSC: 
CFR: 
102517673(SRXN1)
BACU: 
103001633(SRXN1)
LVE: 
103086303(SRXN1)
ECB: 
100067865(SRXN1)
MYB: 
102259833(SRXN1)
MYD: 
102763568(SRXN1)
PALE: 
102883256(SRXN1)
MDO: 
100012125(SRXN1)
SHR: 
100916952(SRXN1)
OAA: 
100089356(SRXN1)
GGA: 
100858692(SRXN1)
APLA: 
TGU: 
100222859(SRXN1)
FAB: 
101815811(SRXN1)
PHI: 
102103918(SRXN1)
FPG: 
101921005(SRXN1)
FCH: 
102057426(SRXN1)
CLV: 
102098754(SRXN1)
ASN: 
102382329(SRXN1)
AMJ: 
102564303(SRXN1)
PSS: 
102459933(SRXN1)
CMY: 
102934189(SRXN1)
ACS: 
103280288(srxn1)
PBI: 
103068041(SRXN1)
DRE: 
100331561(srxn1)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102367152(SRXN1)
CMK: 
103188622(srxn1)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AAG: 
CQU: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
LGI: 
NVE: 
CRE: 
VCN: 
SCE: 
YKL086W(SRX1)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0H03330(NCAS0H03330)
NDI: 
NDAI_0C00330(NDAI0C00330)
TPF: 
TPHA_0L02000(TPHA0L02000)
TBL: 
TBLA_0A00770(TBLA0A00770)
TDL: 
TDEL_0B07360(TDEL0B07360)
KAF: 
KAFR_0C03950(KAFR0C03950)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NPA: 
SPO: 
CNB: 
TMS: 
WSE: 
DPP: 
DFA: 
ACAN: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:14586471]
  Authors
Biteau B, Labarre J, Toledano MB.
  Title
ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.
  Journal
Nature. 425 (2003) 980-4.
  Sequence
[sce:YKL086W]
Reference
2  [PMID:15448164]
  Authors
Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG.
  Title
Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine.
  Journal
J. Biol. Chem. 279 (2004) 50994-1001.
  Sequence
[hsa:140809] [mmu:76650]
Reference
3  [PMID:15590625]
  Authors
Woo HA, Jeong W, Chang TS, Park KJ, Park SJ, Yang JS, Rhee SG.
  Title
Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.
  Journal
J. Biol. Chem. 280 (2005) 3125-8.
  Sequence
[hsa:140809]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
710319-61-2

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