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Literature summary for 1.14.14.21 extracted from

  • Gray, K.A.; Pogrebinsky, O.S.; Mrachko, G.T.; Xi, L.; Monticello, D.J.; Squires, C.H.
    Molecular mechanisms of biocatalytic desulfurization of fossil fuels (1996), Nat. Biotechnol., 14, 1705-1709.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by EDTA Rhodococcus erythropolis

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Rhodococcus erythropolis
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme does not contain Fe2+ or Zn2+, no stimulation by Fe3+, Fe2+, or Cu2+, enzyme DszC does not require a metal cofactor Rhodococcus erythropolis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44977
-
4 * 44977, sequence calculation Rhodococcus erythropolis
180000
-
gel filtration Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dibenzothiophene + 2 FMNH2 + 2 O2 Rhodococcus erythropolis overall reaction dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
dibenzothiophene + 2 FMNH2 + 2 O2 Rhodococcus erythropolis IGTS8 / ATCC 53968 overall reaction dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
dibenzothiophene + FMNH2 + O2 Rhodococcus erythropolis
-
dibenzothiophene-5-oxide + FMN + H2O
-
?
dibenzothiophene + FMNH2 + O2 Rhodococcus erythropolis IGTS8 / ATCC 53968
-
dibenzothiophene-5-oxide + FMN + H2O
-
?
dibenzothiophene-5-oxide + FMNH2 + O2 Rhodococcus erythropolis
-
dibenzothiophene-5,5-dioxide + FMN + H2O
-
?
dibenzothiophene-5-oxide + FMNH2 + O2 Rhodococcus erythropolis IGTS8 / ATCC 53968
-
dibenzothiophene-5,5-dioxide + FMN + H2O
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis A0SWL2 gene dszC
-
Rhodococcus erythropolis IGTS8 / ATCC 53968 A0SWL2 gene dszC
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from strain IGTS8 by dye ligand affinity chromatography, dialysis, and hydrophobic interaction chromatography, followed by gel filtration Rhodococcus erythropolis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dibenzothiophene + 2 FMNH2 + 2 O2 overall reaction Rhodococcus erythropolis dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
dibenzothiophene + 2 FMNH2 + 2 O2 overall reaction Rhodococcus erythropolis IGTS8 / ATCC 53968 dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
dibenzothiophene + FMNH2 + O2
-
Rhodococcus erythropolis dibenzothiophene-5-oxide + FMN + H2O
-
?
dibenzothiophene + FMNH2 + O2
-
Rhodococcus erythropolis IGTS8 / ATCC 53968 dibenzothiophene-5-oxide + FMN + H2O
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
-
Rhodococcus erythropolis dibenzothiophene-5,5-dioxide + FMN + H2O
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
-
Rhodococcus erythropolis IGTS8 / ATCC 53968 dibenzothiophene-5,5-dioxide + FMN + H2O
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 44977, sequence calculation Rhodococcus erythropolis

Synonyms

Synonyms Comment Organism
DBT-MO
-
Rhodococcus erythropolis
DBT-monooxygenase
-
Rhodococcus erythropolis
dszC
-
Rhodococcus erythropolis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Rhodococcus erythropolis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
FMNH2
-
Rhodococcus erythropolis
NADH the enzyme does not directly react with NADH, but uses the activity of the FMN:NADH oxidoreductase, DszD Rhodococcus erythropolis

General Information

General Information Comment Organism
metabolism strain IGTS8 has the ability to convert dibenzothiophene to 2-hydroxybiphenyl with the release of inorganic sulfur. The conversion of dibenzothiophene to 2-hydroxybiphenyl is catalyzed by a multienzyme pathway consisting of two monooxygenases and a desulfinase. The final reaction catalyzed by the desulfinase DszB appears to be the rate limiting step in the pathway Rhodococcus erythropolis