KEGG   ENZYME: 1.13.11.18Help
Entry
EC 1.13.11.18               Enzyme                                 

Name
persulfide dioxygenase;
sulfur oxygenase (incorrect);
sulfur:oxygen oxidoreductase (incorrect);
sulfur dioxygenase (incorrect)
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname
S-sulfanylglutathione:oxygen oxidoreductase
Reaction(IUBMB)
S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+ (overall reaction) [RN:R00781];
(1a) S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+ [RN:R08677];
(1b) S-sulfinatoglutathione + H2O = glutathione + sulfite + H+ (spontaneous) [RN:R08678]
Reaction(KEGG)
Substrate
S-sulfanylglutathione [CPD:C17267];
O2 [CPD:C00007];
H2O [CPD:C00001];
S-sulfinatoglutathione
Product
glutathione [CPD:C00051];
sulfite [CPD:C00094];
H+ [CPD:C00080];
S-sulfinatoglutathione
Comment
An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
History
EC 1.13.11.18 created 1972, modified 2015
Pathway
Sulfur metabolism
Microbial metabolism in diverse environments
Orthology
K17725  
sulfur dioxygenase
Genes
HSA: 
23474(ETHE1)
PTR: 
456093(ETHE1)
GGO: 
101138346(ETHE1)
PON: 
100458034(ETHE1)
NLE: 
100607326(ETHE1)
MCC: 
718089(ETHE1)
MCF: 
102135821(ETHE1)
RRO: 
104669456(ETHE1)
CJC: 
100392539(ETHE1)
MMU: 
66071(Ethe1)
RNO: 
292710(Ethe1)
CGE: 
100769786(Ethe1)
NGI: 
103749149(Ethe1)
HGL: 
101700567(Ethe1)
OCU: 
100340123(ETHE1)
TUP: 
102495095(ETHE1)
CFA: 
612416(ETHE1)
AML: 
100470121(ETHE1)
UMR: 
103657004(ETHE1)
FCA: 
101092565(ETHE1)
PTG: 
102966568(ETHE1)
BTA: 
509150(ETHE1)
BOM: 
102274866(ETHE1)
PHD: 
102330175(ETHE1)
CHX: 
102183356(ETHE1)
OAS: 
101108154(ETHE1)
SSC: 
100523003(ETHE1)
CFR: 
102515553(ETHE1)
BACU: 
103015695(ETHE1)
LVE: 
103088914(ETHE1)
ECB: 
100146195(ETHE1)
MYB: 
102243740(ETHE1)
MYD: 
102751781(ETHE1)
PALE: 
102885174(ETHE1)
SHR: 
100919768(ETHE1)
OAA: 
107546927(ETHE1)
GGA: 
CJO: 
107307773(ETHE1)
PHI: 
102114459(XRCC1) 106628866(ETHE1)
ASN: 
102372675(ETHE1)
AMJ: 
102565248(ETHE1)
CMY: 
ACS: 
100561649(ethe1)
PBI: 
103054622(ETHE1)
GJA: 
107122195(ETHE1)
XLA: 
379091(ethe1)
XTR: 
448221(ethe1)
DRE: 
405865(ethe1)
TRU: 
101079181(ethe1)
MZE: 
OLA: 
101159221(ethe1)
XMA: 
LCM: 
102365540(ETHE1)
BFO: 
CIN: 
SPU: 
SKO: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD25902(Dsim_GD25902) Dsimw501_GD28368(Dsim_GD28368)
DWI: 
DYA: 
Dyak_GE13523(dyak_GLEANR_13725)
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
SOC: 
AEC: 
HST: 
CFO: 
NVI: 
TCA: 
BMOR: 
PXY: 
API: 
PHU: 
ISC: 
CEL: 
CBR: 
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
CRG: 
OBI: 
SMM: 
NVE: 
HMG: 
ATH: 
AT1G53580(GLY3)
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
EGR: 
GMX: 
PVU: 
VRA: 
MTR: 
CAM: 
ADU: 
AIP: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
POPTR_0001s38910g(POPTRDRAFT_749057) POPTR_0005s22640g(POPTRDRAFT_831572)
VVI: 
SLY: 
SPEN: 
SOT: 
SIND: 
BVG: 
NNU: 
OSA: 
DOSA: 
Os01t0667200-01(Os01g0667200)
OBR: 
BDI: 
SBI: 
SORBI_03g030620(SORBIDRAFT_03g030620)
ZMA: 
100283164(IDP546)
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
OLU: 
OTA: 
BPG: 
MIS: 
MPP: 
GSL: 
PTI: 
TPS: 
NGD: 
EHX: 
GTT: 
NGR: 
 » show all
Taxonomy
Reference
1  [PMID:5968172]
  Authors
Suzuki I, Silver M.
  Title
The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli.
  Journal
Biochim. Biophys. Acta. 122 (1966) 22-33.
Reference
2  [PMID:12855721]
  Authors
Rohwerder T, Sand W.
  Title
The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp.
  Journal
Microbiology. 149 (2003) 1699-710.
Reference
3  [PMID:24389926]
  Authors
Liu H, Xin Y, Xun L
  Title
Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria.
  Journal
Appl. Environ. Microbiol. 80 (2014) 1799-806.
Reference
4  [PMID:22786886]
  Authors
Holdorf MM, Owen HA, Lieber SR, Yuan L, Adams N, Dabney-Smith C, Makaroff CA
  Title
Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development.
  Journal
Plant. Physiol. 160 (2012) 226-36.
  Sequence
[ath:AT1G53580]
Reference
5  [PMID:25596185]
  Authors
Pettinati I, Brem J, McDonough MA, Schofield CJ
  Title
Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy.
  Journal
Hum. Mol. Genet. 24 (2015) 2458-69.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37256-58-9

DBGET integrated database retrieval system