Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1 increases the catalytic activity of enzyme DszC 3.5fold compared to the activity with Rhodococcus erythropolis strain D-1 flavin reductase. The flavin reductase from Vibrio harveyi is also stimulating. Analysis and comparison of flavin reductase and DBT monooxygenase activity with purified DszC and cell-free extracts from several non-DBT-desulfurizing microorganisms, overview. In the microbial DBT desulfurization, flavin reductase from the non-DBT-desulfurizing bacterium is superior to that from the DBT-desulfurizing bacterium, The flavin reductase is best active with FMN, but also with FAD, riboflavin, and nitrofurazone | Rhodococcus erythropolis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dibenzothiophene + 2 FMNH2 + 2 O2 | Rhodococcus erythropolis | - |
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
dibenzothiophene + 2 FMNH2 + 2 O2 | Rhodococcus erythropolis D-1 | - |
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus erythropolis | A0A0C6DRW4 | gene dszC | - |
Rhodococcus erythropolis D-1 | A0A0C6DRW4 | gene dszC | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dibenzothiophene + 2 FMNH2 + 2 O2 | - |
Rhodococcus erythropolis | dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
dibenzothiophene + 2 FMNH2 + 2 O2 | - |
Rhodococcus erythropolis D-1 | dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
additional information | analysis of the coupled reaction of DszC with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview | Rhodococcus erythropolis | ? | - |
? | |
additional information | analysis of the coupled reaction of DszC with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview | Rhodococcus erythropolis D-1 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DBT monooxygenase | - |
Rhodococcus erythropolis |
dszC | - |
Rhodococcus erythropolis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 35 | assay at | Rhodococcus erythropolis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Rhodococcus erythropolis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMNH2 | - |
Rhodococcus erythropolis |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in the dibenzothiophene desulfurizing metabolizing dibenzothiophene to form 2-hydroxybiphenyl without breaking the carbon skeleton, dibenzothiophene desulfurization pathway, overview | Rhodococcus erythropolis |
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 | Rhodococcus erythropolis |