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Literature summary for 1.14.14.21 extracted from

  • Li, J.; Feng, J.; Li, Q.; Ma, C.; Yu, B.; Gao, C.; Wu, G.; Xu, P.
    Both FMNH2 and FADH2 can be utilized by the dibenzothiophene monooxygenase from a desulfurizing bacterium Mycobacterium goodii X7B (2009), Biores. Technol., 100, 2594-2599.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
FAD stimulates enzyme DszC activity significantly at 0.01 mM, best at 0.035 mM Mycobacterium goodii
FMN stimulates enzyme DszC activity significantly at 0.001 mM, best at 0.005 mM Mycobacterium goodii

Cloned(Commentary)

Cloned (Comment) Organism
gene dszC, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3) Mycobacterium goodii

Inhibitors

Inhibitors Comment Organism Structure
FAD the flavin at high concentrations inhibits the activity of DszC due to autocatalytic oxidation of reduced flavin, formation of H2O2 Mycobacterium goodii
FMN the flavin at high concentrations inhibits the activity of DszC due to autocatalytic oxidation of reduced flavin, formation of H2O2 Mycobacterium goodii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
x * 45000, recombinant enzyme, SDS-PAGE Mycobacterium goodii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dibenzothiophene + 2 FMNH2 + 2 O2 Mycobacterium goodii
-
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
dibenzothiophene + 2 FMNH2 + 2 O2 Mycobacterium goodii X7B
-
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium goodii B2CML6 gene dszC
-
Mycobacterium goodii X7B B2CML6 gene dszC
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) Mycobacterium goodii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dibenzothiophene + 2 FADH2 + 2 O2
-
Mycobacterium goodii dibenzothiophene-5,5-dioxide + 2 FAD + 2 H2O
-
?
dibenzothiophene + 2 FADH2 + 2 O2
-
Mycobacterium goodii X7B dibenzothiophene-5,5-dioxide + 2 FAD + 2 H2O
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
-
Mycobacterium goodii dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
-
Mycobacterium goodii X7B dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
?
additional information the recombinant enzyme is able to utilize either FMNH2 or FADH2 when coupled with a flavin reductase that reduces either FMN or FAD. Autocatalytic oxidation of reduced flavins, overview Mycobacterium goodii ?
-
?
additional information the recombinant enzyme is able to utilize either FMNH2 or FADH2 when coupled with a flavin reductase that reduces either FMN or FAD. Autocatalytic oxidation of reduced flavins, overview Mycobacterium goodii X7B ?
-
?

Subunits

Subunits Comment Organism
? x * 45000, recombinant enzyme, SDS-PAGE Mycobacterium goodii

Synonyms

Synonyms Comment Organism
DBT monooxygenase
-
Mycobacterium goodii
dibenzothiophene monooxygenase
-
Mycobacterium goodii
dszC
-
Mycobacterium goodii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mycobacterium goodii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Mycobacterium goodii

Cofactor

Cofactor Comment Organism Structure
FADH2
-
Mycobacterium goodii
FMNH2
-
Mycobacterium goodii
additional information the recombinant enzyme is able to utilize either FMNH2 or FADH2 when coupled with a flavin reductase that reduces either FMN or FAD Mycobacterium goodii

General Information

General Information Comment Organism
evolution sequence analysis indicates that DszC is similar to the C2 component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii, which can use both FADH2 and FMNH2 as substrates. The monooxygenase components might be divided into three subclasses: the strictly FMNH2-utilizing subclass, the strictly FADH2-utilizing subclass, and the FMNH2 and FADH2 both-utilizing subclass. DszC has the acyl-CoA dehydrogenase folding and experimentally proves to be able to use both FMNH2 and FADH2 as the substrate, therefore, DszC belongs to the FMNH2 and FADH2 both utilizing subclass, phylogenetic analysis of monooxygenase components of the two-component flavin-dependent monooxygenases Mycobacterium goodii