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
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Metals Ions
Metals Ions on EC 1.13.11.18 - persulfide dioxygenase
for references in articles please use BRENDA:EC1.13.11.18
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Fe2+
Iron
non-heme iron
additional information
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required, the PDO domain active site contains a mononuclear non-heme iron coordinated by His58, His114, and Asp133 comprising a 2His:1Asp facial triad. The remaining coordination sites are occupied by water molecules giving an octrahedral geometry around ferrous iron. The wild-type enzyme contains 0.60 mol iron per mol of enzyme, the mutant C314S 0.46 mol iron/mol enzyme
the eukaryotic mitochondrial sulfur dioxygenases metal II binding site is conserved but no metal binding is observed
additional information
the eukaryotic mitochondrial sulfur dioxygenases metal II binding site is conserved but no metal binding is observed
additional information
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the eukaryotic mitochondrial sulfur dioxygenases metal II binding site is conserved but no metal binding is observed