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1-methyldibenzothiophene + 2 FMNH2 + 2 O2
1-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
2,7-diethylbenzothiophene + FMNH2 + O2
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
2-ethylbenzothiophene + FMNH2 + O2
?
2-ethyldibenzothiophene + 2 FMNH2 + 2 O2
2-ethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
2-methylbenzothiophene + FMNH2 + O2
?
2-methyldibenzothiophene + 2 FMNH2 + 2 O2
2-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
3,4,6,7-tetramethyldibenzothiophene + 2 FMNH2 + 2 O2
3,4,6,7-tetramethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
3,4,6-trimethyldibenzothiophene + 2 FMNH2 + 2 O2
3,4,6-trimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
3,4-benzo-dibenzothiophene + 2 FMNH2 + 2 O2
3,4-benzo-dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
3-ethyldibenzothiophene + 2 FMNH2 + 2 O2
3-ethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
3-methylbenzothiophene + 2 FMNH2 + 2 O2
3-methylbenzothiophene-1,1-dioxide + 2 FMN + 2 H2O
-
-
-
?
3-methylbenzothiophene + FMNH2 + O2
?
-
less than 10% of the activity with dibenzothiophene
-
-
?
3-methyldibenzothiophene + 2 FMNH2 + 2 O2
3-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
4,6-diethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-diethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
4-methyldibenzothiophene + 2 FMNH2 + 2 O2
4-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
5-methylbenzothiophene + 2 FMNH2 + 2 O2
5-methylbenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
5-methylbenzothiophene + FMNH2 + O2
?
-
33% of the activity with dibenzothiophene
-
-
?
7-ethylbenzothiophene + FMNH2 + O2
?
-
less than 10% of the activity with dibenzothiophene
-
-
?
benzothiophene + 2 FMNH2 + 2 O2
benzothiophene-5,5-dioxide + 2 FMN + 2 H2O
dibenzothiophene + 2 FADH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FAD + 2 H2O
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
dibenzothiophene + 2 reduced riboflavin + 2 O2
dibenzothiophene-5,5-dioxide + 2 riboflavin + 2 H2O
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
thioxanthen-9-one + 2 FMNH2 + 2 O2
?
thioxanthen-9-one + FMNH2 + O2
?
additional information
?
-
2,7-diethylbenzothiophene + FMNH2 + O2
?
-
13% of the activity with dibenzothiophene
-
-
?
2,7-diethylbenzothiophene + FMNH2 + O2
?
-
13% of the activity with dibenzothiophene
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
best substrate
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
129% of the activity with dibenzothiophene
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
129% of the activity with dibenzothiophene
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
best substrate
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
2-ethylbenzothiophene + FMNH2 + O2
?
-
28% of the activity with dibenzothiophene
-
-
?
2-ethylbenzothiophene + FMNH2 + O2
?
-
28% of the activity with dibenzothiophene
-
-
?
2-ethyldibenzothiophene + 2 FMNH2 + 2 O2
2-ethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
2-ethyldibenzothiophene + 2 FMNH2 + 2 O2
2-ethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
2-methylbenzothiophene + FMNH2 + O2
?
-
209% of the activity with dibenzothiophene
-
-
?
2-methylbenzothiophene + FMNH2 + O2
?
-
209% of the activity with dibenzothiophene
-
-
?
2-methyldibenzothiophene + 2 FMNH2 + 2 O2
2-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
2-methyldibenzothiophene + 2 FMNH2 + 2 O2
2-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
3,4,6,7-tetramethyldibenzothiophene + 2 FMNH2 + 2 O2
3,4,6,7-tetramethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
3,4,6,7-tetramethyldibenzothiophene + 2 FMNH2 + 2 O2
3,4,6,7-tetramethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
3,4-benzo-dibenzothiophene + 2 FMNH2 + 2 O2
3,4-benzo-dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
3,4-benzo-dibenzothiophene + 2 FMNH2 + 2 O2
3,4-benzo-dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
low activity
-
-
?
3,4-benzo-dibenzothiophene + 2 FMNH2 + 2 O2
3,4-benzo-dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
low activity
-
-
?
3-methyldibenzothiophene + 2 FMNH2 + 2 O2
3-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
3-methyldibenzothiophene + 2 FMNH2 + 2 O2
3-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
4,6-diethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-diethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
4,6-diethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-diethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
low activity
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
low activity
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
52% of the activity with dibenzothiophene
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
52% of the activity with dibenzothiophene
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
4-methyldibenzothiophene + 2 FMNH2 + 2 O2
4-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
4-methyldibenzothiophene + 2 FMNH2 + 2 O2
4-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
4-methyldibenzothiophene + 2 FMNH2 + 2 O2
4-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
low activity
-
-
?
4-methyldibenzothiophene + 2 FMNH2 + 2 O2
4-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
low activity
-
-
?
4-methyldibenzothiophene + 2 FMNH2 + 2 O2
4-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
benzothiophene + 2 FMNH2 + 2 O2
benzothiophene-5,5-dioxide + 2 FMN + 2 H2O
best substrate
-
-
?
benzothiophene + 2 FMNH2 + 2 O2
benzothiophene-5,5-dioxide + 2 FMN + 2 H2O
best substrate
-
-
?
benzothiophene + 2 FMNH2 + 2 O2
benzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FADH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FAD + 2 H2O
-
-
-
?
dibenzothiophene + 2 FADH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FAD + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
low reactivity of TdsC toward dibenzothiophene at high substrate concentrations
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
low reactivity of TdsC toward dibenzothiophene at high substrate concentrations
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
best substrate
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
high activity
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
high activity
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 reduced riboflavin + 2 O2
dibenzothiophene-5,5-dioxide + 2 riboflavin + 2 H2O
overall reaction, low activity with riboflavin
-
-
?
dibenzothiophene + 2 reduced riboflavin + 2 O2
dibenzothiophene-5,5-dioxide + 2 riboflavin + 2 H2O
overall reaction, low activity with riboflavin
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
thioxanthen-9-one + 2 FMNH2 + 2 O2
?
-
-
-
-
?
thioxanthen-9-one + 2 FMNH2 + 2 O2
?
-
-
-
?
thioxanthen-9-one + FMNH2 + O2
?
45% of the activity with dibenzothiophene
-
-
?
thioxanthen-9-one + FMNH2 + O2
?
45% of the activity with dibenzothiophene
-
-
?
additional information
?
-
-
coupled reaction with flavin reductase (TdsD) from thermophilic Paenibacillus sp. strain A11-2. Substrate specificity, overview. No activity with 4,6-di-n-propyl-DBT, 4,6-di-n-butyl-DBT, carbazole, dibenzofuran, fluorene, biphenyl, DBT sulfone, benzothiophene, and naphthothiophene
-
-
?
additional information
?
-
-
the enzyme utilizes aromatic compounds, not having sulfur atoms, as substrates. It acts on indole, converting it to indoxyl and isatin, and its derivatives to form indigoid pigments, and also utilizes indoline and phenoxazine. Indigo derivative formation by BdsC using methylindoles as substrates. Enzyme BdsC exhibits activity toward benzothiophene derivatives but not benzothiophene itself showing a wide reactivity toward aromatic compounds. To measure BdsC activity, flavin reductase (DszD) from another desulfurizing species, Rhodococcus erythropolis strain D-1, is used. Sulfone formations, product analysis by GC-MS
-
-
?
additional information
?
-
-
the enzyme utilizes aromatic compounds, not having sulfur atoms, as substrates. It acts on indole, converting it to indoxyl and isatin, and its derivatives to form indigoid pigments, and also utilizes indoline and phenoxazine. Indigo derivative formation by BdsC using methylindoles as substrates. Enzyme BdsC exhibits activity toward benzothiophene derivatives but not benzothiophene itself showing a wide reactivity toward aromatic compounds. To measure BdsC activity, flavin reductase (DszD) from another desulfurizing species, Rhodococcus erythropolis strain D-1, is used. Sulfone formations, product analysis by GC-MS
-
-
?
additional information
?
-
-
coupled reaction with flavin reductase (TdsD) from thermophilic Paenibacillus sp. strain A11-2. Substrate specificity, overview. No activity with 4,6-di-n-propyl-DBT, 4,6-di-n-butyl-DBT, carbazole, dibenzofuran, fluorene, biphenyl, DBT sulfone, benzothiophene, and naphthothiophene
-
-
?
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
-
-
?
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
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-
?
additional information
?
-
-
the dszC gene encodes DBT monooxygenase, which catalyzes the conversion of dibenzothiophene to dibenzothiophene sulfone
-
-
?
additional information
?
-
-
the dszC gene encodes DBT monooxygenase, which catalyzes the conversion of dibenzothiophene to dibenzothiophene sulfone
-
-
?
additional information
?
-
substrate specificity of enzyme TsdC with dibenzothiophene derivatives and benzothiophene derivatives, overview. No or poor activity with 4,6-dipropyldibenzothiophene, 4,6-dibutyldibenzothiophene, and 1-methyldibenzothiophene
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-
?
additional information
?
-
substrate specificity of enzyme TsdC with dibenzothiophene derivatives and benzothiophene derivatives, overview. No or poor activity with 4,6-dipropyldibenzothiophene, 4,6-dibutyldibenzothiophene, and 1-methyldibenzothiophene
-
-
?
additional information
?
-
-
FMN:NADPH oxidoreductase from Vibrio harveyi complements activities of purified DszA and DszC proteins. DszA and DszC are oxygenase units that do not use NAD(P)H directly, but instead use FMNH2 from a FMN:NADPH oxidoreductase for oxygenation. The oxygenase and oxidoreductase units do not interact but exchange electrons, overview. Purified DszC or DszA proteins exhibit no activity in presence of 10 mM FMN, 5 mM NADPH, oxygen, and organosulfur substrates
-
-
?
additional information
?
-
strain KA2-5-1 desulfurizes a variety of alkyl dibenzothiophenes through the specific cleavage of their C-S bonds. In addition, strain KA2-5-1 also attacks alkyl benzothiophenes in a C-S-bond-targeted fashion, substrate specificity overview
-
-
?
additional information
?
-
analysis of the coupled reaction of DszC with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview
-
-
?
additional information
?
-
coupled assay with endogenous NADH-dependent flavin reductase, EC 1.5.1.36
-
-
?
additional information
?
-
no or poor activity with 3,4-benzo-dibenzothiophene, biphenyl, carbazole, dibenzofuran, and fluorene, substrate specificity, overview. Interaction with purified flavin reductase from the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, with DszC
-
-
?
additional information
?
-
purified enzyme DszC couples in the reaction with a flavin reductase purified from Bacillus sp. strain DSM411, the flavin reductase reacts with FMN and NADH, but also with NADPH and FAD to a lesser extent
-
-
?
additional information
?
-
the purified monooxygenase, encoded by dszC of KA2-5-1, converts benzothiophene and dibenzothiophene into benzothiophene sulfone and dibenzothiophene sulfone, respectively, with the aid of an NADH-dependent oxidoreductase, substrate specificity overview
-
-
?
additional information
?
-
purified enzyme DszC couples in the reaction with a flavin reductase purified from Bacillus sp. strain DSM411, the flavin reductase reacts with FMN and NADH, but also with NADPH and FAD to a lesser extent
-
-
?
additional information
?
-
coupled assay with endogenous NADH-dependent flavin reductase, EC 1.5.1.36
-
-
?
additional information
?
-
analysis of the coupled reaction of DszC with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview
-
-
?
additional information
?
-
no or poor activity with 3,4-benzo-dibenzothiophene, biphenyl, carbazole, dibenzofuran, and fluorene, substrate specificity, overview. Interaction with purified flavin reductase from the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, with DszC
-
-
?
additional information
?
-
-
FMN:NADPH oxidoreductase from Vibrio harveyi complements activities of purified DszA and DszC proteins. DszA and DszC are oxygenase units that do not use NAD(P)H directly, but instead use FMNH2 from a FMN:NADPH oxidoreductase for oxygenation. The oxygenase and oxidoreductase units do not interact but exchange electrons, overview. Purified DszC or DszA proteins exhibit no activity in presence of 10 mM FMN, 5 mM NADPH, oxygen, and organosulfur substrates
-
-
?
additional information
?
-
strain KA2-5-1 desulfurizes a variety of alkyl dibenzothiophenes through the specific cleavage of their C-S bonds. In addition, strain KA2-5-1 also attacks alkyl benzothiophenes in a C-S-bond-targeted fashion, substrate specificity overview
-
-
?
additional information
?
-
the purified monooxygenase, encoded by dszC of KA2-5-1, converts benzothiophene and dibenzothiophene into benzothiophene sulfone and dibenzothiophene sulfone, respectively, with the aid of an NADH-dependent oxidoreductase, substrate specificity overview
-
-
?
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
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-
?
additional information
?
-
reduced FMN reacts with an oxygen molecule at C4a position of the isoalloxazine ring, producing the C4a-(hydro)peroxyflavin intermediate which is stabilized by residues H391 and S163. H391 may contribute to the formation of the C4a-(hydro)peroxyflavin by acting as a proton donor to the proximal peroxy oxygen, and it might also be involved in the protonation process of the C4a-(hydro)xyflavin, substrate binding and mechanism, molecular docking
-
-
?
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
-
-
?
additional information
?
-
reduced FMN reacts with an oxygen molecule at C4a position of the isoalloxazine ring, producing the C4a-(hydro)peroxyflavin intermediate which is stabilized by residues H391 and S163. H391 may contribute to the formation of the C4a-(hydro)peroxyflavin by acting as a proton donor to the proximal peroxy oxygen, and it might also be involved in the protonation process of the C4a-(hydro)xyflavin, substrate binding and mechanism, molecular docking
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
2-ethyldibenzothiophene + 2 FMNH2 + 2 O2
2-ethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
3,4,6,7-tetramethyldibenzothiophene + 2 FMNH2 + 2 O2
3,4,6,7-tetramethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
3,4,6-trimethyldibenzothiophene + 2 FMNH2 + 2 O2
3,4,6-trimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
3-ethyldibenzothiophene + 2 FMNH2 + 2 O2
3-ethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
4,6-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
4-methyldibenzothiophene + 2 FMNH2 + 2 O2
4-methyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
benzothiophene + 2 FMNH2 + 2 O2
benzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
additional information
?
-
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
2,8-dimethyldibenzothiophene + 2 FMNH2 + 2 O2
2,8-dimethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
2-ethyldibenzothiophene + 2 FMNH2 + 2 O2
2-ethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
2-ethyldibenzothiophene + 2 FMNH2 + 2 O2
2-ethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
3,4,6,7-tetramethyldibenzothiophene + 2 FMNH2 + 2 O2
3,4,6,7-tetramethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
3,4,6,7-tetramethyldibenzothiophene + 2 FMNH2 + 2 O2
3,4,6,7-tetramethyldibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
best substrate
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
overall reaction
-
-
?
dibenzothiophene + 2 FMNH2 + 2 O2
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O
-
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene + FMNH2 + O2
dibenzothiophene-5-oxide + FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
dibenzothiophene-5-oxide + FMNH2 + O2
dibenzothiophene-5,5-dioxide + FMN + H2O
-
-
-
?
additional information
?
-
-
the dszC gene encodes DBT monooxygenase, which catalyzes the conversion of dibenzothiophene to dibenzothiophene sulfone
-
-
?
additional information
?
-
-
the dszC gene encodes DBT monooxygenase, which catalyzes the conversion of dibenzothiophene to dibenzothiophene sulfone
-
-
?
additional information
?
-
-
FMN:NADPH oxidoreductase from Vibrio harveyi complements activities of purified DszA and DszC proteins. DszA and DszC are oxygenase units that do not use NAD(P)H directly, but instead use FMNH2 from a FMN:NADPH oxidoreductase for oxygenation. The oxygenase and oxidoreductase units do not interact but exchange electrons, overview. Purified DszC or DszA proteins exhibit no activity in presence of 10 mM FMN, 5 mM NADPH, oxygen, and organosulfur substrates
-
-
?
additional information
?
-
strain KA2-5-1 desulfurizes a variety of alkyl dibenzothiophenes through the specific cleavage of their C-S bonds. In addition, strain KA2-5-1 also attacks alkyl benzothiophenes in a C-S-bond-targeted fashion, substrate specificity overview
-
-
?
additional information
?
-
-
FMN:NADPH oxidoreductase from Vibrio harveyi complements activities of purified DszA and DszC proteins. DszA and DszC are oxygenase units that do not use NAD(P)H directly, but instead use FMNH2 from a FMN:NADPH oxidoreductase for oxygenation. The oxygenase and oxidoreductase units do not interact but exchange electrons, overview. Purified DszC or DszA proteins exhibit no activity in presence of 10 mM FMN, 5 mM NADPH, oxygen, and organosulfur substrates
-
-
?
additional information
?
-
strain KA2-5-1 desulfurizes a variety of alkyl dibenzothiophenes through the specific cleavage of their C-S bonds. In addition, strain KA2-5-1 also attacks alkyl benzothiophenes in a C-S-bond-targeted fashion, substrate specificity overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
DszC with specificity for FMN makes a unique member of the flavin monooxygenase family
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
evolution
-
DszC with specificity for FMN makes a unique member of the flavin monooxygenase family
-
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
-
malfunction
site-directed mutagenesis study shows that mutations in the residues involved either in catalysis or in flavin or substrate-binding result in a complete loss of enzyme activity, suggesting that the accurate positions of flavin and substrate are crucial for the enzyme activity
malfunction
-
site-directed mutagenesis study shows that mutations in the residues involved either in catalysis or in flavin or substrate-binding result in a complete loss of enzyme activity, suggesting that the accurate positions of flavin and substrate are crucial for the enzyme activity
-
metabolism
-
DBT monooxygenase from Rhodococcus erythropolis is involved in the first step of the 4S pathway. Dibenzothiophene and its derivatives are resistant to the hydrodesulfurization method often used in industry, but they are susceptible to enzymatic desulfurization via the 4S pathway
metabolism
-
dibenzothiophene is converted to 2'-hydroxybiphenyl-2-sulfinate by ec1.14.14.21 and 1.14.14.22 in strain F.5.25.8, and the 2'-hydroxybiphenyl-2-sulfinate concentration does not decrease during the stationary phase. Although the production of 2'-hydroxybiphenyl-2-sulfinate appears to proceed in parallel with the increase in biomass, the relationship between the decrease in dibenzothiophene and increase in 2'-hydroxybiphenyl-2-sulfinate does not seem stoichiometric due to the volatile nature of 2'-hydroxybiphenyl-2-sulfinate
metabolism
dibenzothiophene monooxygenase is the first enzyme involved in the degradation of dibenzothiophene
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
metabolism
the DBT monooxygenase from Rhodococcus erythropolis D-1 is involved in the first two steps of the 4S pathway. The 4S metabolic pathway catalyzes the sequential conversion of DBT to 2'-hydroxybiphenyl via three enzymes encoded by the dsz operon in several bacterial species
metabolism
-
the dibenzothiophene (DBT) desulfurization enzyme system consists of three enzymes: DBT monooxygenase, DBT sulfone monooxygenase, and 2'-hydroxybiphenyl 2-sulfinate desulfinase
metabolism
the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1
metabolism
the enzyme is involved in the dibenzothiophene desulfurizing metabolizing dibenzothiophene to form 2-hydroxybiphenyl without breaking the carbon skeleton, dibenzothiophene desulfurization pathway, overview
metabolism
the enzyme is involved in the pathway of microbial dibenzothiophene desulfurization, overview
metabolism
-
dibenzothiophene is converted to 2'-hydroxybiphenyl-2-sulfinate by ec1.14.14.21 and 1.14.14.22 in strain F.5.25.8, and the 2'-hydroxybiphenyl-2-sulfinate concentration does not decrease during the stationary phase. Although the production of 2'-hydroxybiphenyl-2-sulfinate appears to proceed in parallel with the increase in biomass, the relationship between the decrease in dibenzothiophene and increase in 2'-hydroxybiphenyl-2-sulfinate does not seem stoichiometric due to the volatile nature of 2'-hydroxybiphenyl-2-sulfinate
-
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
-
metabolism
-
the dibenzothiophene (DBT) desulfurization enzyme system consists of three enzymes: DBT monooxygenase, DBT sulfone monooxygenase, and 2'-hydroxybiphenyl 2-sulfinate desulfinase
-
metabolism
-
dibenzothiophene monooxygenase is the first enzyme involved in the degradation of dibenzothiophene
-
metabolism
-
the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1
-
metabolism
-
the enzyme is involved in the dibenzothiophene desulfurizing metabolizing dibenzothiophene to form 2-hydroxybiphenyl without breaking the carbon skeleton, dibenzothiophene desulfurization pathway, overview
-
metabolism
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the DBT monooxygenase from Rhodococcus erythropolis D-1 is involved in the first two steps of the 4S pathway. The 4S metabolic pathway catalyzes the sequential conversion of DBT to 2'-hydroxybiphenyl via three enzymes encoded by the dsz operon in several bacterial species
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metabolism
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the enzyme is involved in the pathway of microbial dibenzothiophene desulfurization, overview
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physiological function
DszC and DszA catalyze monooxygenation reactions in the desulfurization of dibenzothiophene, both requiring the additional enzyme flavin reductase, which catalyzes the reduction of flavin by NAD(P)H to form reduced flavin
physiological function
flavin reductase or flavin-dependent monooxygenase efficiently couples with the other component in two-component monooxygenases. Coexpression of frb with the DBT-desulfurization genes (bdsABC) from Bacillus subtilis strain WU-S2B is critical for high DBT-desulfurizing ability over a wide temperature range of 20-55°C
physiological function
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Mycobacterium phlei strain GTIS10 converts dibenzothiophene to 2'-hydroxybiphenyl, determination of metabolites from dibenzothiophene, overview
physiological function
the dibenzothiophene (DBT) monooxygenase DszC, which is the key initiating enzyme in 4S metabolic pathway, catalyzes sequential sulphoxidation reaction of DBT to DBT sulfoxide (DBTO), then DBT sulfone (DBTO2). Residues H391, and D392 directly participate in catalysis. Residues H92, Y96, N129, F161, S163, W205, R282, R370, and H388 are involved in flavin or substrate-binding
physiological function
the dibenzothiophene (DBT)-desulfurizing bacterium, Rhodococcus erythropolis D-1, removes sulfur from dibenzothiophene to form 2-hydroxybiphenyl using four enzymes, DszC, DszA, DszB, and flavin reductase
physiological function
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Mycobacterium phlei strain GTIS10 converts dibenzothiophene to 2'-hydroxybiphenyl, determination of metabolites from dibenzothiophene, overview
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physiological function
-
the dibenzothiophene (DBT) monooxygenase DszC, which is the key initiating enzyme in 4S metabolic pathway, catalyzes sequential sulphoxidation reaction of DBT to DBT sulfoxide (DBTO), then DBT sulfone (DBTO2). Residues H391, and D392 directly participate in catalysis. Residues H92, Y96, N129, F161, S163, W205, R282, R370, and H388 are involved in flavin or substrate-binding
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physiological function
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flavin reductase or flavin-dependent monooxygenase efficiently couples with the other component in two-component monooxygenases. Coexpression of frb with the DBT-desulfurization genes (bdsABC) from Bacillus subtilis strain WU-S2B is critical for high DBT-desulfurizing ability over a wide temperature range of 20-55°C
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physiological function
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the dibenzothiophene (DBT)-desulfurizing bacterium, Rhodococcus erythropolis D-1, removes sulfur from dibenzothiophene to form 2-hydroxybiphenyl using four enzymes, DszC, DszA, DszB, and flavin reductase
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physiological function
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DszC and DszA catalyze monooxygenation reactions in the desulfurization of dibenzothiophene, both requiring the additional enzyme flavin reductase, which catalyzes the reduction of flavin by NAD(P)H to form reduced flavin
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additional information
C-terminal DBT-binding site by using a molecular docking simulation that simultaneously docks the FMN cofactor and DBT substrate to an apo-DszC structure, role of the C terminus in catalysis
additional information
flavin reductase (DszD) is essential for the enzyme activity of DszC
additional information
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the C-terminus (410-417) of enzyme DszC, which is located in the interior of the protein, is important for the stabilization of the active conformation of the substrate-binding pocket and the tetrameric state and plays a significant role in the catalytic activity of the enzyme. The residues around the site are conserved: Tyr96, Asn129, Phe161, Ser163, Trp205, Ser215, Phe250, and His391
additional information
two distinct conformations occur in the flexible lid loops adjacent to the active site (residue 280-295, between helix alpha9 and alpha10), that are named open and closed state, respectively, and might show the status of the free and ligand-bound DszC
additional information
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two distinct conformations occur in the flexible lid loops adjacent to the active site (residue 280-295, between helix alpha9 and alpha10), that are named open and closed state, respectively, and might show the status of the free and ligand-bound DszC
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additional information
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flavin reductase (DszD) is essential for the enzyme activity of DszC
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additional information
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C-terminal DBT-binding site by using a molecular docking simulation that simultaneously docks the FMN cofactor and DBT substrate to an apo-DszC structure, role of the C terminus in catalysis
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71
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2004
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