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Literature summary extracted from
- Both FMNH2 and FADH2 can be utilized by the dibenzothiophene monooxygenase from a desulfurizing bacterium Mycobacterium goodii X7B (2009), Biores. Technol., 100, 2594-2599.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.21 | FAD | stimulates enzyme DszC activity significantly at 0.01 mM, best at 0.035 mM | Mycobacterium goodii |  |
| 1.14.14.21 | FMN | stimulates enzyme DszC activity significantly at 0.001 mM, best at 0.005 mM | Mycobacterium goodii | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.21 | gene dszC, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3) | Mycobacterium goodii |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.21 | FAD | the flavin at high concentrations inhibits the activity of DszC due to autocatalytic oxidation of reduced flavin, formation of H2O2 | Mycobacterium goodii | |
| 1.14.14.21 | 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]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.21 | 45000 | - |
x * 45000, recombinant enzyme, SDS-PAGE | Mycobacterium goodii |
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 | Mycobacterium goodii | - |
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
| 1.14.14.21 | dibenzothiophene + 2 FMNH2 + 2 O2 | Mycobacterium goodii X7B | - |
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.21 | Mycobacterium goodii | B2CML6 | gene dszC | - |
| 1.14.14.21 | Mycobacterium goodii X7B | B2CML6 | gene dszC | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.21 | recombinant enzyme from Escherichia coli strain BL21(DE3) | Mycobacterium goodii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.21 | dibenzothiophene + 2 FADH2 + 2 O2 | - |
Mycobacterium goodii | dibenzothiophene-5,5-dioxide + 2 FAD + 2 H2O | - |
? | |
| 1.14.14.21 | dibenzothiophene + 2 FADH2 + 2 O2 | - |
Mycobacterium goodii X7B | dibenzothiophene-5,5-dioxide + 2 FAD + 2 H2O | - |
? | |
| 1.14.14.21 | dibenzothiophene + 2 FMNH2 + 2 O2 | - |
Mycobacterium goodii | dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
| 1.14.14.21 | dibenzothiophene + 2 FMNH2 + 2 O2 | - |
Mycobacterium goodii X7B | dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
| 1.14.14.21 | 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 | ? | - |
? | |
| 1.14.14.21 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.14.21 | ? | x * 45000, recombinant enzyme, SDS-PAGE | Mycobacterium goodii |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.21 | DBT monooxygenase | - |
Mycobacterium goodii |
| 1.14.14.21 | dibenzothiophene monooxygenase | - |
Mycobacterium goodii |
| 1.14.14.21 | dszC | - |
Mycobacterium goodii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.21 | 37 | - |
assay at | Mycobacterium goodii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.21 | 7 | - |
assay at | Mycobacterium goodii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.21 | FADH2 | - |
Mycobacterium goodii | |
| 1.14.14.21 | FMNH2 | - |
Mycobacterium goodii | |
| 1.14.14.21 | 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
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.14.21 | 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 |
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