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Literature summary extracted from

  • Lei, B.; Tu, S.C.
    Gene overexpression, purification, and identification of a desulfurization enzyme from Rhodococcus sp. strain IGTS8 as a sulfide/sulfoxide monooxygenase (1996), J. Bacteriol., 178, 5699-5705.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.21 gene sox/dszC, overexpression in Escherichia coli strain BL21 Rhodococcus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.21 45000
-
2 * 45000, recombinant enzyme, SDS-PAGE Rhodococcus sp.
1.14.14.21 86000
-
recombinant enzyme, gel filtration Rhodococcus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.21 dibenzothiophene + 2 FMNH2 + 2 O2 Rhodococcus sp. overall reaction dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
1.14.14.21 dibenzothiophene + 2 FMNH2 + 2 O2 Rhodococcus sp. IGTS8 overall reaction dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
1.14.14.21 dibenzothiophene + FMNH2 + O2 Rhodococcus sp.
-
dibenzothiophene-5-oxide + FMN + H2O
-
?
1.14.14.21 dibenzothiophene + FMNH2 + O2 Rhodococcus sp. IGTS8
-
dibenzothiophene-5-oxide + FMN + H2O
-
?
1.14.14.21 dibenzothiophene-5-oxide + FMNH2 + O2 Rhodococcus sp.
-
dibenzothiophene-5,5-dioxide + FMN + H2O
-
?
1.14.14.21 dibenzothiophene-5-oxide + FMNH2 + O2 Rhodococcus sp. IGTS8
-
dibenzothiophene-5,5-dioxide + FMN + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.21 Rhodococcus sp. P54998 gene sox/dszC
-
1.14.14.21 Rhodococcus sp. IGTS8 P54998 gene sox/dszC
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.21 recombinant enzyme from Escherichia coli strain BL21 by anion exchange and hydrophobic interaction chromatography, followed by dialysis Rhodococcus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.21 dibenzothiophene + 2 FMNH2 + 2 O2 overall reaction Rhodococcus sp. dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
1.14.14.21 dibenzothiophene + 2 FMNH2 + 2 O2 overall reaction Rhodococcus sp. IGTS8 dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
1.14.14.21 dibenzothiophene + 2 reduced riboflavin + 2 O2 overall reaction, low activity with riboflavin Rhodococcus sp. dibenzothiophene-5,5-dioxide + 2 riboflavin + 2 H2O
-
?
1.14.14.21 dibenzothiophene + 2 reduced riboflavin + 2 O2 overall reaction, low activity with riboflavin Rhodococcus sp. IGTS8 dibenzothiophene-5,5-dioxide + 2 riboflavin + 2 H2O
-
?
1.14.14.21 dibenzothiophene + FMNH2 + O2
-
Rhodococcus sp. dibenzothiophene-5-oxide + FMN + H2O
-
?
1.14.14.21 dibenzothiophene + FMNH2 + O2
-
Rhodococcus sp. IGTS8 dibenzothiophene-5-oxide + FMN + H2O
-
?
1.14.14.21 dibenzothiophene-5-oxide + FMNH2 + O2
-
Rhodococcus sp. dibenzothiophene-5,5-dioxide + FMN + H2O
-
?
1.14.14.21 dibenzothiophene-5-oxide + FMNH2 + O2
-
Rhodococcus sp. IGTS8 dibenzothiophene-5,5-dioxide + FMN + H2O
-
?
1.14.14.21 additional information dibenzothiophene sulfoxide and sulfone obtain their oxygen atom(s) from molecular oxygen rather than water in their formation from dibenzothiophene, isotope labeling. The enzyme also utilizes benzyl sulfide and benzyl sulfoxide as substrates, it is a sulfide/sulfoxide monooxygenase. A flavin reductase FRP coupled assay Rhodococcus sp. ?
-
?
1.14.14.21 additional information dibenzothiophene sulfoxide and sulfone obtain their oxygen atom(s) from molecular oxygen rather than water in their formation from dibenzothiophene, isotope labeling. The enzyme also utilizes benzyl sulfide and benzyl sulfoxide as substrates, it is a sulfide/sulfoxide monooxygenase. A flavin reductase FRP coupled assay Rhodococcus sp. IGTS8 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.14.14.21 homodimer 2 * 45000, recombinant enzyme, SDS-PAGE Rhodococcus sp.

Synonyms

EC Number Synonyms Comment Organism
1.14.14.21 dszC
-
Rhodococcus sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.21 FMNH2 the enzyme binds one flavin mononucleotide or reduced flavin mononucleotide (FMNH2) per 90,200-Da homodimer, and FMNH2 is an essential cosubstrate for its activity Rhodococcus sp.
1.14.14.21 additional information flavin reductaseFRP is essentially required for enzyme activity providing reduction equivalents, Vibrio harveyi FRP produces FMNH2 at the expense of NADPH and is used to provide FMNH2 for the enzymatic reaction Rhodococcus sp.
1.14.14.21 additional information flavin specificity, overview. No activity with FADH2 Rhodococcus sp.
1.14.14.21 riboflavin low activity Rhodococcus sp.