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Literature summary extracted from
- Flavin reductase coupling with two monooxygenases involved in dibenzothiophene desulfurization: purification and characterization from a non-desulfurizing bacterium, Paenibacillus polymyxa A-1 (2002), Appl. Microbiol. Biotechnol., 59, 649-657.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.21 | 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 | |
| 1.14.14.22 | additional information | NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1 increases the catalytic activity of enzyme DszA 5fold compared to the activity with Rhodococcus erythropolis strain D-1 flavin reductase. The flavin reuctase from Vibrio harveyi is also stimulating. In the microbial DBT-desulfurization, flavin reductase from the non-DBT-desulfurizing bacterium is superior to that from the DBT-desulfurizing bacterium | Rhodococcus erythropolis |
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 erythropolis | - |
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? |  |
| 1.14.14.21 | dibenzothiophene + 2 FMNH2 + 2 O2 | Rhodococcus erythropolis D-1 | - |
dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
| 1.14.14.22 | dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2 | Rhodococcus erythropolis | - |
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O | - |
? | |
| 1.14.14.22 | dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2 | Rhodococcus erythropolis D-1 | - |
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.21 | Rhodococcus erythropolis | A0A0C6DRW4 | gene dszC | - |
| 1.14.14.21 | Rhodococcus erythropolis D-1 | A0A0C6DRW4 | gene dszC | - |
| 1.14.14.22 | Rhodococcus erythropolis | Q6WE15 | gene dszA | - |
| 1.14.14.22 | Rhodococcus erythropolis D-1 | Q6WE15 | gene dszA | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.21 | dibenzothiophene + 2 FMNH2 + 2 O2 | - |
Rhodococcus erythropolis | dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
| 1.14.14.21 | dibenzothiophene + 2 FMNH2 + 2 O2 | - |
Rhodococcus erythropolis D-1 | dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O | - |
? | |
| 1.14.14.21 | additional information | analysis of the coupled reaction of DszC with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview | Rhodococcus erythropolis | ? | - |
? | |
| 1.14.14.21 | 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 | ? | - |
? | |
| 1.14.14.22 | dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2 | - |
Rhodococcus erythropolis | 2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O | - |
? | |
| 1.14.14.22 | dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2 | - |
Rhodococcus erythropolis D-1 | 2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O | - |
? | |
| 1.14.14.22 | additional information | analysis of the coupled reaction of DszA with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview | Rhodococcus erythropolis | ? | - |
? | |
| 1.14.14.22 | additional information | analysis of the coupled reaction of DszA with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview | Rhodococcus erythropolis D-1 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.21 | DBT monooxygenase | - |
Rhodococcus erythropolis |
| 1.14.14.21 | dszC | - |
Rhodococcus erythropolis |
| 1.14.14.22 | DBT sulfone monooxygenase | - |
Rhodococcus erythropolis |
| 1.14.14.22 | dszA | - |
Rhodococcus erythropolis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.21 | 30 | 35 | assay at | Rhodococcus erythropolis |
| 1.14.14.22 | 30 | 35 | assay at | Rhodococcus erythropolis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.21 | 7 | - |
assay at | Rhodococcus erythropolis |
| 1.14.14.22 | 7 | - |
assay at | Rhodococcus erythropolis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.21 | FMNH2 | - |
Rhodococcus erythropolis | |
| 1.14.14.22 | FMNH2 | - |
Rhodococcus erythropolis | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.14.21 | 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 |
| 1.14.14.21 | 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 |
| 1.14.14.22 | 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 |
| 1.14.14.22 | 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 |
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