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Literature summary for 1.14.14.21 extracted from

  • Ohshiro, T.; Aoi, Y.; Torii, K.; Izumi, Y.
    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.
    View publication on PubMed
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Activating Compound

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Rhodococcus erythropolis A0A0C6DRW4 gene dszC
-
Rhodococcus erythropolis D-1 A0A0C6DRW4 gene dszC
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
DBT monooxygenase
-
 Rhodococcus erythropolis
dszC
-
 Rhodococcus erythropolis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 35 assay at Rhodococcus erythropolis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
FMNH2
-
 Rhodococcus erythropolis

General Information

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