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, physiological 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)
CSAB: 103215990(SRXN1)
RRO: 104660811(SRXN1)
RBB: 108544558(SRXN1)
CJC: 100386992(SRXN1)
SBQ: 101043399(SRXN1)
MMU: 76650(Srxn1)
RNO: 296271(Srxn1)
CGE: 100759653(Srxn1)
NGI: 103751626(Srxn1)
HGL: 101726463(Srxn1)
CCAN: 109687014(Srxn1)
OCU: 100359116(SRXN1)
TUP: 102471871(SRXN1)
CFA: 100686728(SRXN1)
AML: 100473816(SRXN1)
UMR: 103674490(SRXN1)
ORO: 101372818(SRXN1)
FCA: 101090507(SRXN1)
PTG: 102956412(SRXN1)
AJU: 106985978(SRXN1)
BTA: 531606(SRXN1)
BOM: 102264913(SRXN1)
BIU: 109567331(SRXN1)
PHD: 102334004(SRXN1)
CHX: 102180685(SRXN1)
OAS: 101121699(SRXN1)
SSC: 100517736(SRXN1)
CFR: 102517673(SRXN1)
CDK: 105100802(SRXN1)
BACU: 103001633(SRXN1)
LVE: 103086303(SRXN1)
OOR: 101283749(SRXN1)
ECB: 100067865(SRXN1)
EPZ: 103556919(SRXN1)
MYB: 102259833(SRXN1)
MYD: 102763568(SRXN1)
HAI: 109384433(SRXN1)
RSS: 109460111(SRXN1)
PALE: 102883256(SRXN1)
LAV: 100655164(SRXN1)
MDO: 100012125(SRXN1)
SHR: 100916952(SRXN1)
OAA: 100089356(SRXN1)
GGA: 100858692(SRXN1)
MGP: 104914015(SRXN1)
CJO: 107323173(SRXN1)
TGU: 100222859(SRXN1)
GFR: 102035740(SRXN1)
FAB: 101815811(SRXN1)
PHI: 102103918(SRXN1)
PMAJ: 107213136(SRXN1)
CCAE: 111938130(SRXN1)
FPG: 101921005(SRXN1)
FCH: 102057426(SRXN1)
CLV: 102098754(SRXN1)
ASN: 102382329(SRXN1)
AMJ: 102564303(SRXN1)
CMY: 102934189(SRXN1)
CPIC: 101932001(SRXN1)
ACS: 103280288(srxn1)
PVT: 110086046(SRXN1)
PBI: 103068041(SRXN1)
GJA: 107109820(SRXN1)
NPR: 108786987(SRXN1)
DRE: 100331561(srxn1)
SRX: 107711830(srxn1)
SANH: 107680324(srxn1)
SGH: 107594516(srxn1)
CCAR: 109083350(srxn1)
IPU: 108264881(srxn1)
AMEX: 103029943(srxn1)
TRU: 101063345(srxn1)
LCO: 104919946(srxn1)
NCC: 104943988(srxn1)
MZE: 101487142(srxn1)
XMA: 102218601(srxn1)
PRET: 103467763(srxn1)
KMR: 108249563(srxn1)
LCF: 108890476(srxn1)
BPEC: 110164815(srxn1)
SASA: 106567196(srxn1)
OTW: 112221419(srxn1)
ELS: 105022325(srxn1)
SFM: 108939220(srxn1)
LCM: 102367152(SRXN1)
CMK: 103188622(srxn1)
CIN: 100185108
SPU: 764239
APLC: 110975776
SKO: 100377903
DME: Dmel_CG6762(CG6762)
DER: 6550168
DPE: 6597572
DSI: Dsimw501_GD17370(Dsim_GD17370)
DWI: 6649225
MDE: 101889303
AAG: 5578621
BIM: 105680425
SOC: 105195926
AEC: 105150043
ACEP: 105620649
PBAR: 105426939
HST: 105182533
DQU: 106745483
CFO: 105253157
LHU: 105670259
PCF: 106785213
MDL: 103576855
TCA: 663169
DPA: 109535847
NVL: 108566869
BMOR: 101735518
PMAC: 106711988
PRAP: 110991803
HAW: 110374621
PXY: 105398636
API: 100161553
DNX: 107170591
ZNE: 110832200
TUT: 107362143
CRG: 105322669
OBI: 106871679
LAK: 106176400
ADF: 107352059
ATH: AT1G31170(SRX)
CRB: 17898306
BRP: 103833827
BOE: 106325136
THJ: 104798553
CPAP: 110817809
CIT: 102612116
TCC: 18607054
GRA: 105763059
DZI: 111298228
EGR: 104445793
GMX: 100527425
VRA: 106766966
VAR: 108334637
CCAJ: 109806087
CAM: 101497213
LJA: Lj4g3v0654390.1(Lj4g3v0654390.1) Lj5g3v0309110.1(Lj5g3v0309110.1)
ADU: 107484129
AIP: 107639269
LANG: 109341411
FVE: 101291900
PPER: 18779336
PMUM: 103325453
PAVI: 110770623
MDM: 103435288
ZJU: 107425505
CSV: 101217757
CMO: 103498252
MCHA: 111012631
RCU: 8289489
JCU: 105629049
HBR: 110632536
POP: 7453987
JRE: 109003588
VVI: 100245605
SLY: 101260008
SPEN: 107011242
SOT: 102592429
CANN: 107857945
NSY: 104216162
NTO: 104089833
INI: 109147294
SIND: 105175880
OEU: 111370425
HAN: 110895872
LSV: 111882054
CCAV: 112512707
DCR: 108204245
BVG: 104892382
SOE: 110784360
NNU: 104599677
OSA: 9268874
DOSA: Os06t0174300-01(Os06g0174300)
OBR: 102719394
BDI: 100838881
ATS: 109752607(LOC109752607)
SBI: 8076174
SITA: 101770539
EGU: 105056125
MUS: 103978725
DCT: 110110974
PEQ: 110023413
AOF: 109833405
ATR: 18448098
PPP: 112284903
CRE: CHLREDRAFT_96296(SRX1)
APRO: F751_3028
SCE: YKL086W(SRX1)
ERC: Ecym_3406
KMX: KLMA_60166(SRX1)
NCS: NCAS_0H03330(NCAS0H03330)
NDI: NDAI_0C00330(NDAI0C00330)
TPF: TPHA_0L02000(TPHA0L02000)
TBL: TBLA_0A00770(TBLA0A00770)
TDL: TDEL_0B07360(TDEL0B07360)
KAF: KAFR_0C03950(KAFR0C03950)
CAL: CAALFM_C205060CA(CaO19.3537)
CAUR: QG37_02641
SPO: SPBC106.02c(srx1)
CNB: CNBA6150
DFA: DFA_09143
 » 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 425:980-4 (2003)
DOI:10.1038/nature02075
  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 279:50994-1001 (2004)
DOI:10.1074/jbc.M409482200
  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 280:3125-8 (2005)
DOI:10.1074/jbc.C400496200
  Sequence
[hsa:140809]
Other DBs
ExplorEnz - The Enzyme Database: 1.8.98.2
IUBMB Enzyme Nomenclature: 1.8.98.2
ExPASy - ENZYME nomenclature database: 1.8.98.2
BRENDA, the Enzyme Database: 1.8.98.2
CAS: 710319-61-2

DBGET integrated database retrieval system