1.13.11.18: persulfide dioxygenase
This is an abbreviated version!
For detailed information about persulfide dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.18
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1.13.11.18
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social
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ethylmalonic
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encephalopathy
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attitudes
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authoritarianism
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right-wing
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prejudice
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ideology
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thiosulfate
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intergroup
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petechia
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acrocyanosis
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political
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rhodanese
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polysulfides
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sulfide:quinone
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inequality
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group-based
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orthostatic
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conservatism
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lesbian
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cross-lagged
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endorsement
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pseudaminobacter
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1-hydroxy-2-naphthoate
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ingroup
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medicine
- 1.13.11.18
-
social
-
ethylmalonic
- encephalopathy
-
attitudes
-
authoritarianism
-
right-wing
-
prejudice
-
ideology
- thiosulfate
-
intergroup
-
petechia
-
acrocyanosis
-
political
- rhodanese
- polysulfides
-
sulfide:quinone
-
inequality
-
group-based
-
orthostatic
-
conservatism
-
lesbian
-
cross-lagged
-
endorsement
-
pseudaminobacter
- 1-hydroxy-2-naphthoate
-
ingroup
- medicine
Reaction
Synonyms
AFE_0269, BAE27_01805, BpPRF, cPDO-PT, CstB, ETHE1, ETHE1-like sulfur dioxygenase, Ethe2, Fe(II)-containing persulfide dioxygenase, Gly3, PDO, PRF, SDO, SOR, sulfide dioxygenase, sulfur dioxygenase, sulfur oxygenase, sulfur oxygenase/reductase
ECTree
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Substrates Products
Substrates Products on EC 1.13.11.18 - persulfide dioxygenase
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REACTION DIAGRAM
gamma-glutamyl-homocysteinyl-glycine + O2
gamma-glutamyl-homocysteinyl-SO2H + ?
mechanism-based inhibitor, accepted as an alternative substrate and converted to glutamyl-homocysteinyl-SO2H
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?
S-sulfanylglutathione + O2
sulfite + glutathione + H+
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?
sulfur + O2 + H2O
thiosulfate
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in the presence of reduced glutathione and 2,2'-dipyridyl
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?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
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incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
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?
5 sulfur + 2 O2 + 2 H2O + 4 H+
sulfite + thiosulfate + 2 sulfide
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incorporation of elemental sulfur, possible role in thiosulfate metabolism, reaction provides energy
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?
S-sulfanylglutathione + O2 + H2O
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r
glutathione + sulfite + 2 H+
S-sulfanylglutathione + O2 + H2O
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r
glutathione + sulfite + 2 H+
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r
sulfite
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low amount of thiosulfate observed may result from a chemical reaction between sulfite and elemental sulfur
ir
sulfur + O2 + H2O
sulfite
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-
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
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?
sulfur + O2 + H2O
sulfite
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incorporation of elemental sulfur
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
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?
sulfur + O2 + H2O
sulfite
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further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
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?
sulfur + O2 + H2O
sulfite
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incorporation of elemental sulfur
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
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?
sulfur + O2 + H2O
sulfite
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further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
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?
sulfur + O2 + H2O
sulfite
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incorporation of elemental sulfur
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
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?
sulfur + O2 + H2O
sulfite
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S2O32- may be formed through a secondary, non-enzymatic reaction
ir
sulfur + O2 + H2O
sulfite
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-
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
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?
sulfur + O2 + H2O
sulfite
-
incorporation of elemental sulfur
further reacts non-enzymically to form sulfate, thiosulfate or in the presence of glutathione glutathione S-sulfonate
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?
sulfur + O2 + H2O
sulfite
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S2O32- may be formed through a secondary, non-enzymatic reaction
ir
?
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Arabidopsis ETHE1 catalyzes the glutathione persulfide-dependent consumption of oxygen
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?
additional information
?
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BpPRF is a bifunctional enzyme that uses the rhodanese domain to preferentially catalyze sulfur transfer from thiosulfate to GSH to form sulfite and GSSH and uses the PDO domain to oxidize GSSH to sulfite
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?
additional information
?
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cysteine persulfide and thiosulfate are no substrates
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?
additional information
?
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coupled persulfide dioxygenase-persulfide transferase (cPDO-PT) activity assay producing thiosulfate as product preferentially from CoASSH and bacillithiol persulfide. CstB does not catalyze the formation of thiosulfate from reduced low molecular weight thiol, oxidized low molecular weight disulfide or Na2S. Cysteine persulfide (CSSH) and glutathione persulfide (GSSH) also serve as persulfide substrates for wild-type CstB but are poorer substrates
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?
additional information
?
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coupled persulfide dioxygenase-persulfide transferase (cPDO-PT) activity assay producing thiosulfate as product preferentially from CoASSH and bacillithiol persulfide. CstB does not catalyze the formation of thiosulfate from reduced low molecular weight thiol, oxidized low molecular weight disulfide or Na2S. Cysteine persulfide (CSSH) and glutathione persulfide (GSSH) also serve as persulfide substrates for wild-type CstB but are poorer substrates
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?