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Literature summary extracted from

  • Kalimuthu, P.; Kappler, U.; Bernhardt, P.V.
    Catalytic voltammetry of the molybdoenzyme sulfite dehydrogenase from Sinorhizobium meliloti (2014), J. Phys. Chem. B, 118, 7091-7099 .
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.2.1 periplasm
-
Sinorhizobium meliloti
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.2.1 Mo4+ molybdenum enzyme. Sulfite oxidizing enzymes (regardless of origin) share a common active site comprising a dioxido-MoVI moiety chelated by a molybdopterin dithiolene ligand in addition to a cysteinyl S-donor. The equatorial oxido ligand is the one transferred to sulfite during its 2-electron O-atom transfer reaction Sinorhizobium meliloti
1.8.2.1 additional information the enzyme bears no heme cofactor Sinorhizobium meliloti

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.2.1 78000
-
-
Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.2.1 sulfite + 2 ferricytochrome c + H2O Sinorhizobium meliloti
-
sulfate + 2 ferrocytochrome c + 2 H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.8.2.1 Sinorhizobium meliloti
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.2.1 sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+ mechanism of electrochemically mediated, enzyme SorT-catalyzed sulfite oxidation Sinorhizobium meliloti

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.2.1 7.4
-
pH 8.0, 22°C, with horse heart cytochrome c Sinorhizobium meliloti
1.8.2.1 33.4
-
pH 8.0, 22°C, with SorU Sinorhizobium meliloti
1.8.2.1 470
-
pH 8.0, 22°C, with ferricyanide Sinorhizobium meliloti

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.2.1 additional information favorable protein-protein interactions between SorT and c-type cytochrome SorU, i.e. Smc04048, lead to productive electron transfer and catalytic activity. No activity with ferrous horse heart cytochrome c, and no activity with O2 as an sulfite oxidase Sinorhizobium meliloti ?
-
?
1.8.2.1 sulfite + 2 ferricytochrome c + H2O
-
Sinorhizobium meliloti sulfate + 2 ferrocytochrome c + 2 H+
-
?
1.8.2.1 sulfite + 2 ferrocene methanol + H2O
-
Sinorhizobium meliloti sulfate + 2 reduced ferrocene methanol + 2 H+
-
?

Subunits

EC Number Subunits Comment Organism
1.8.2.1 homodimer
-
Sinorhizobium meliloti

Synonyms

EC Number Synonyms Comment Organism
1.8.2.1 SorT
-
Sinorhizobium meliloti

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.2.1 22
-
assay at room temperature Sinorhizobium meliloti

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.8.2.1 22
-
20 min, inactivation Sinorhizobium meliloti

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.2.1 additional information
-
the lack of a plateau prevents the determination of a genuine pH optimum, an apparently linear decrease in activity as a function of pH is not interpretable by standard models of pH-dependent enzyme activity which predict sigmoidal or bell-shaped profiles Sinorhizobium meliloti
1.8.2.1 8
-
assay at Sinorhizobium meliloti

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.8.2.1 6 11 the greatest loss in activity occurs while the enzyme is at pH 10, while in the range above pH 6 and below pH 9 there is no significant variation, inactivation at pH 11.0 Sinorhizobium meliloti

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.8.2.1 11
-
irreversible time-dependent loss of catalytic activity Sinorhizobium meliloti

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.2.1 cytochrome c c-type cytochrome SorU, i.e. Smc04048 Sinorhizobium meliloti
1.8.2.1 additional information ferrocene methanol (in its oxidized ferrocenium form) is utilized as an artificial electron acceptor for the catalytic SorT sulfite oxidation reaction Sinorhizobium meliloti