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Literature summary for 1.14.14.22 extracted from

  • Xi, L.; Squires, C.H.; Monticello, D.J.; Childs, J.D.
    A flavin reductase stimulates DszA and DszC proteins of Rhodococcus erythropolis IGTS8 in vitro (1997), Biochem. Biophys. Res. Commun., 230, 73-75.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2 Rhodococcus erythropolis
-
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2 Rhodococcus erythropolis IGTS8 / ATCC 53968
-
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
?
additional information Rhodococcus erythropolis 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 Rhodococcus erythropolis IGTS8 / ATCC 53968 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis
-
gene dszA
-
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
gene dszA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
-
Rhodococcus erythropolis 2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
-
Rhodococcus erythropolis IGTS8 / ATCC 53968 2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
?
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 Rhodococcus erythropolis ?
-
?
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 Rhodococcus erythropolis IGTS8 / ATCC 53968 ?
-
?

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
30
-
assay at Rhodococcus erythropolis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
FMNH2 the reduced form of flavin serves as a substrate of DszA Rhodococcus erythropolis
additional information no direct activity with NAD(P)H Rhodococcus erythropolis