Disease relevance of LOC396278

• Sulfite oxidase from Thiobacillus novellus has been purified 206-fold [1].
• To test this proposal we carried out radiation inactivation analysis on Escherichia coli DNA polymerase I, Torula yeast glucose-6-phosphate dehydrogenase, Chlorella vulgaris nitrate reductase, and chicken liver sulfite oxidase in the presence and absence of free radical scavengers (benzoic acid and mannitol) [2].

High impact information on LOC396278

• The molybdenum-containing enzyme sulfite oxidase catalyzes the conversion of sulfite to sulfate, the terminal step in the oxidative degradation of cysteine and methionine [3].
• Four variants associated with sulfite oxidase deficiency have been identified: two mutations are near the sulfate binding site, while the other mutations occur within the domain mediating dimerization [3].
• The nature of molybdenum cofactor in the bacterial enzyme dimethyl sulfoxide reductase has been investigated by application of alkylation conditions that convert the molybdenum cofactor in chicken liver sulfite oxidase and milk xanthine oxidase to the stable, well-characterized derivative [di(carboxamidomethyl)]molybdopterin [4].
• Although detailed biochemical analyses have been carried out on these mutations, no structural data could be obtained because of problems in crystallizing recombinant human and rat sulfite oxidases and the failure to clone the chicken sulfite oxidase gene [5].
• We solved the crystal structures of the wild type and the sulfite oxidase deficiency-causing R138Q (R160Q in humans) variant of recombinant chicken sulfite oxidase in the resting and sulfate-bound forms [5].

Chemical compound and disease context of LOC396278

• Purification of Thiobacillus novellus sulfite oxidase. Evidence for the presence of heme and molybdenum [1].

Biological context of LOC396278

• Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase [6].
• Aerobic reactivation of inactive sulfite oxidase required only 1 eq of ferricyanide/active site [7].
• Several point mutations in the sulfite oxidase gene have been identified from patients suffering from this disease worldwide [5].
• YedY is very distinct in overall architecture from all known bacterial reductases but does show some similarity with the catalytic domain of the eukaryotic chicken liver sulfite oxidase [8].
• Chicken liver sulfite oxidase. Kinetics of reduction by laser-photoreduced flavins and intramolecular electron transfer [9].

Associations of LOC396278 with chemical compounds

• The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase [10].
• Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component [11].
• The mechanisms of inactivation of sulfite oxidase by periodate and arsenite [12].
• The release of inorganic phosphate from sulfite oxidase was more rapid (35% in 10 min) due to the presence of molybdate in the denatured enzyme mixture but slower than expected from a high energy phosphate bond [13].
• The phosphate is noncovalently bound but is not released by trichloroacetic acid at 4 degrees C. The yield of Form A and Form B from sulfite oxidase is 0.50 and 0.27/subunit, respectively [13].

Physical interactions of LOC396278

• There are two equal and non-interacting cytochrome c binding sites per sulfite oxidase monomer [14].

Enzymatic interactions of LOC396278

• The mitochondrial enzyme sulfite oxidase catalyzes the oxidation of cytochrome c by sulfite [14].

Other interactions of LOC396278

• Similar dissociation constants were measured for the binding of these anions by flash photolysis and by steady-state enzyme kinetics using the inhibition of the sulfite/cytochrome c assay reaction for sulfite oxidase [15].
• COX, sulfite oxidase, xanthine oxidase, and xanthine dehydrogenase each contains 2 mol of molybdopterin per mol of enzyme [16].

Analytical, diagnostic and therapeutic context of LOC396278

• Moreover, analysis of the visible absorption spectrum of the purified enzyme and the co-elution of 413 and 280 nm absorbing material during high pressure liquid chromatography gel chromatography provided clear evidence for the presence of heme in T. novellus sulfite oxidase [1].
• We synthesized the gene for chicken sulfite oxidase de novo, working backward from the amino acid sequence of the native chicken liver enzyme by PCR amplification of a series of 72 overlapping primers [5].
• With one dithiolene and one thiolate ligand of a square pyramidal Mo(VI)O(2)S(3) coordination unit, 9 closely resembles the oxidized sites in sulfite oxidase and assimilatory nitrate reductase as deduced from crystallography (sulfite oxidase) and Mo EXAFS [17].
• The titration of chicken liver sulfite oxidase (SO) with the one-electron reductant Ti(III) citrate, at pH 7.0, results in nearly quantitative selective reduction of the Mo(VI) center to Mo(V), while the b-type heme center remains in the fully oxidized Fe(III) state [18].
• An improved method for the purification of sulfite oxidase from chicken liver, using affinity chromatography on cytochrome c--Sepharose, is described [14].

References