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Literature summary for 1.13.11.55 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
Search for more literature for 1.13.11.55

Activating Compound

Activating Compound Comment Organism Structure
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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Inhibitors

Inhibitors Comment Organism Structure
Hg2+ blocks cysteines in the active site pocket Acidianus ambivalens
iodoacetic acid blocks cysteines in the active site pocket Acidianus ambivalens
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

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

Metals/Ions

Metals/Ions Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
Acidianus ambivalens P29082 gene sor
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
SOR
-
 Acidianus ambivalens
sulfur oxygenase reductase
-
 Acidianus ambivalens

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
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
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