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:1.13.11.49
Description:Chlorite O(2)-lyase.
Alternative Name: Chlorite dismutase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.13.11.49
BRENDA Enzyme Link: BRENDA 1.13.11.49
KEGG Enzyme Link: KEGG1.13.11.49
BioCyc Enzyme Link: BioCyc 1.13.11.49
ExPASy Enzyme Link: ExPASy1.13.11.49
EC2PDB Enzyme Link: EC2PDB 1.13.11.49
ExplorEnz Enzyme Link: ExplorEnz 1.13.11.49
PRIAM enzyme-specific profiles Link: PRIAM 1.13.11.49
IntEnz Enzyme Link: IntEnz 1.13.11.49
MEDLINE Enzyme Link: MEDLINE 1.13.11.49
MSA:

1.13.11.49;

Phylogenetic Tree:

1.13.11.49;

Uniprot:
M-CSA:
RHEA:21404 chloride + O2 = chlorite
RULE(radius=1) [Cl-;H0:1].[O;H0;+0:2]=[O;H0;+0:3]>>[O;H0;+0:2]=[ClH+3:1]-[OH;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and characterization of chlorite dismutase: a novel oxygen-generating enzyme.van Ginkel CG, Rikken GB, Kroon AG, Kengen SW1996 Nov8929278
Structural and functional characterisation of the chlorite dismutase from the nitrite-oxidizing bacterium "Candidatus Nitrospira defluvii": identification of a catalytically important amino acid residue.Kostan J, Sjöblom B, Maixner F, Mlynek G, Furtmüller PG, Obinger C, Wagner M, Daims H, Djinović-Carugo K2010 Dec20600954
Mechanism of and exquisite selectivity for O-O bond formation by the heme-dependent chlorite dismutase.Lee AQ, Streit BR, Zdilla MJ, Abu-Omar MM, DuBois JL2008 Oct 1418840691
Chemical and steady-state kinetic analyses of a heterologously expressed heme dependent chlorite dismutase.Streit BR, DuBois JL2008 May 1318422344
Chlorite dismutase from Ideonella dechloratans.Stenklo K, Thorell HD, Bergius H, Aasa R, Nilsson T2001 Jun11472023