Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.14.22 extracted from

  • Matsubara, T.; Ohshiro, T.; Nishina, Y.; Izumi, Y.
    Purification, characterization, and overexpression of flavin reductase involved in dibenzothiophene desulfurization by Rhodococcus erythropolis D-1 (2001), Appl. Environ. Microbiol., 67, 1179-1184.
    View publication on PubMedView publication on EuropePMC

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 D-1
-
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis Q6WE15 gene dszA
-
Rhodococcus erythropolis D-1 Q6WE15 gene dszA
-

Source Tissue

Source Tissue Comment Organism Textmining
cell culture grown on dibenzothiophene as sole sulfur source Rhodococcus erythropolis
-

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 D-1 2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
?

Synonyms

Synonyms Comment Organism
DBT sulfone monooxygenase
-
Rhodococcus erythropolis
dszA
-
Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
FMNH2
-
Rhodococcus erythropolis
additional information the flavin reductase, EC 1.5.1.36, from Rhodococcus erythropolis strain D-1 grown in a medium containing dibenzothiophene as the sole source of sulfur is essential for the reactions of the two monooxygenases DszC and DszA in vivo. The purified flavin reductase contains no chromogenic cofactors and has a molecular mass of 86 kDa and four identical 22-kDa subunits. The enzyme catalyzes NADH-dependent reduction of flavin mononucleotide, FMN. The flavin reductase does not catalyze reduction of any nitroaromatic compound Rhodococcus erythropolis

General Information

General Information Comment Organism
metabolism the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1 Rhodococcus erythropolis
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 Rhodococcus erythropolis