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Literature summary extracted from

  • Veith, A.; Urich, T.; Seyfarth, K.; Protze, J.; Frazao, C.; Kletzin, A.
    Substrate pathways and mechanisms of inhibition in the sulfur oxygenase reductase of Acidianus ambivalens (2011), Front. Microbiol., 2, 37.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.13.11.55 additional information opening the putative substrate and product pathways in the outer shell leads to a significant increase in specific activity and to a shift in the stoichiometry of the products Acidianus ambivalens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.55 gene sor, sequence comparisons, expression in Escherichia coli strain BL21 Codon plus (DE3) RIL Acidianus ambivalens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.11.55 X-ray crystallography of SOR wild-type crystals soaked with inhibitors Hg2+ and iodoacetamide, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, crystal structure analysis Acidianus ambivalens

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.55 F133A site-directed mutagenesis of a tetramer channel residue, the mutant shows reduced activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 F133A/F141A site-directed mutagenesis of a tetramer channel residue, the mutant shows increased activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 F141A site-directed mutagenesis of a tetramer channel residue, the mutant shows increased activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 H166A site-directed mutagenesis of the zinc site residue, the mutant shows reduced activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 H277A site-directed mutagenesis of the zinc site residue, the mutant shows activity similar to the wild-type enzyme Acidianus ambivalens
1.13.11.55 M296V site-directed mutagenesis of the active site pore residue, the mutant shows slightly increased activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 M297A site-directed mutagenesis of the active site pore residue, the mutant shows reduced activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 MM296/297TT site-directed mutagenesis of the active site pore residue, the mutant shows reduced activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 MM296/297VT site-directed mutagenesis of the active site pore residue, the mutant shows reduced activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 additional information modeling of active site pore mutants based on the wild-type structure, overview Acidianus ambivalens
1.13.11.55 R99A site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 R99I site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 S226A site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 S226I site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 S226L site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme Acidianus ambivalens
1.13.11.55 S226T site-directed mutagenesis of a trimer channel residue, the mutant shows increased activity compared to the wild-type enzyme Acidianus ambivalens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.55 Hg2+ blocks cysteines in the active site pocket Acidianus ambivalens
1.13.11.55 iodoacetic acid blocks cysteines in the active site pocket Acidianus ambivalens
1.13.11.55 Zn2+ zinc binds far from the actIve sIte , Zn2+ interferes over a distance with the subunit pores in the outer shell, possibly by restriction of protein flexibility or substrate access or product exit Acidianus ambivalens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.13.11.55 cytoplasm
-
 Acidianus ambivalens 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.55 Fe2+ non-heme iron. The iron site and the three conserved cysteine residues are located in an active site pocket that is connected to the inner cavity of the sphere by a narrow pore formed by two adjacent methionines and a phenylalanine Acidianus ambivalens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.55 4 sulfur + 4 H2O + O2 Acidianus ambivalens
-
 2 hydrogen sulfide + 2 bisulfite + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.55 Acidianus ambivalens P29082 gene sor
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.55 4 sulfur + 4 H2O + O2
-
 Acidianus ambivalens 2 hydrogen sulfide + 2 bisulfite + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.55 tetraeicosamer dodecamer of dimers, modeling of the SOR and its pores, overview Acidianus ambivalens

Synonyms

EC Number Synonyms Comment Organism
1.13.11.55 SOR
-
 Acidianus ambivalens
1.13.11.55 sulfur oxygenase reductase
-
 Acidianus ambivalens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.55 22
-
 assay at room temperature Acidianus ambivalens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.55 7.2
-
 assay at Acidianus ambivalens

General Information

EC Number General Information Comment Organism
1.13.11.55 metabolism sulfur oxygenase reductase is the initial enzyme of the sulfur oxidation pathway in the thermoacidophilic Archaeon Acidianus ambivalens catalyzing an oxygen-dependent sulfur disproportionation to H2S, sulfite and thiosulfate Acidianus ambivalens
1.13.11.55 additional information the spherical, hollow, cytoplasmic enzyme is composed of 24 identical subunits with an active site pocket each comprising a mononuclear non-heme iron site and a cysteine persulfide. Substrate access and product exit occur via apolar chimney-like protrusions at the fourfold symmetry axes, via narrow polar pores at the threefold symmetry axes and via narrow apolar pores within in each subunit. The expansion of the pores in the outer shell leads to an increased enzyme activity while the integrity of the active site pore seems to be important. The iron site and the three conserved cysteine residues are located in an active site pocket that is connected to the inner cavity of the sphere by a narrow pore formed by two adjacent methionines and a phenylalanine. Modeling of the SOR and its pores, overview. Opening the putative substrate and product pathways in the outer shell leads to a significant increase in specific activity and to a shift in the stoichiometry of the products Acidianus ambivalens