Enzyme

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     1. Oxidoreductases
        1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
            1.13.11 With incorporation of two atoms of oxygen
ID:1.13.11.18
Description:Persulfide dioxygenase.
Alternative Name: Sulfur oxygenase.
Sulfur dioxygenase.
Cath: 3.60.15.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.13.11.18
BRENDA Enzyme Link: BRENDA 1.13.11.18
KEGG Enzyme Link: KEGG1.13.11.18
BioCyc Enzyme Link: BioCyc 1.13.11.18
ExPASy Enzyme Link: ExPASy1.13.11.18
EC2PDB Enzyme Link: EC2PDB 1.13.11.18
ExplorEnz Enzyme Link: ExplorEnz 1.13.11.18
PRIAM enzyme-specific profiles Link: PRIAM 1.13.11.18
IntEnz Enzyme Link: IntEnz 1.13.11.18
MEDLINE Enzyme Link: MEDLINE 1.13.11.18
MSA:

1.13.11.18;

Phylogenetic Tree:

1.13.11.18;

Uniprot:
M-CSA:
RHEA:12981 H2O + O2 + S-sulfanylglutathione = glutathione + 2 H(+) + sulfite
RULE(radius=1) [*:1]-[S;H0;+0:2]-[SH;+0:3].[O;H0;+0:4]=[O;H0;+0:5].[OH2;+0:6]>>[*:1]-[SH;+0:2].[O;H0;+0:4]=[S;H0;+0:3](-[OH;+0:5])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy.Pettinati I, Brem J, McDonough MA, Schofield CJ2015 May 125596185
Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria.Liu H, Xin Y, Xun L2014 Mar24389926
Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism.Kabil O, Banerjee R2012 Dec 2823144459
Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development.Holdorf MM, Owen HA, Lieber SR, Yuan L, Adams N, Dabney-Smith C, Makaroff CA2012 Sep22786886
Loss of ETHE1, a mitochondrial dioxygenase, causes fatal sulfide toxicity in ethylmalonic encephalopathy.Tiranti V, Viscomi C, Hildebrandt T, Di Meo I, Mineri R, Tiveron C, Levitt MD, Prelle A, Fagiolari G, Rimoldi M, Zeviani M2009 Feb19136963
The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp.Rohwerder T, Sand W2003 Jul12855721