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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.30
-
Rhodococcus erythropolis

General Stability

EC Number General Stability Organism
1.5.1.30 stable at temperatures below 50°C Rhodococcus erythropolis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.30 7-hydroxycoumarin
-
Rhodococcus erythropolis
1.5.1.30 Ag+
-
Rhodococcus erythropolis
1.5.1.30 Cu2+
-
Rhodococcus erythropolis
1.5.1.30 Hg+
-
Rhodococcus erythropolis
1.5.1.30 NEM when the enzyme is preincubated with NEM and NADH in the absence of FMN Rhodococcus erythropolis
1.5.1.30 p-chloromercuribenzoic acid
-
Rhodococcus erythropolis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.30 0.0108
-
FMN
-
Rhodococcus erythropolis
1.5.1.30 0.208
-
NADH
-
Rhodococcus erythropolis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.30 22000
-
4 * 22000, SDS-PAGE Rhodococcus erythropolis
1.5.1.30 86000
-
gel filtration 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
1.5.1.30 Rhodococcus erythropolis
-
D1
-
1.5.1.30 Rhodococcus erythropolis D1
-
D1
-
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
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.30
-
Rhodococcus erythropolis

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.30 122
-
-
Rhodococcus erythropolis
1.5.1.30 133
-
flavin reductase from recombinant Escherichia coli Rhodococcus erythropolis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.30 FMN + NADPH
-
Rhodococcus erythropolis FMNH2 + NADP+
-
?
1.5.1.30 FMN + NADPH
-
Rhodococcus erythropolis D1 FMNH2 + NADP+
-
?
1.5.1.30 riboflavin-5-phosphate + NADH + H+
-
Rhodococcus erythropolis reduced FMN + NAD+
-
r
1.5.1.30 riboflavin-5-phosphate + NADH + H+
-
Rhodococcus erythropolis D1 reduced FMN + NAD+
-
r
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 coupled assay with endogenous NADH-dependent flavin reductase, EC 1.5.1.36 Rhodococcus erythropolis ?
-
?
1.14.14.21 additional information coupled assay with endogenous NADH-dependent flavin reductase, EC 1.5.1.36 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
-
?

Subunits

EC Number Subunits Comment Organism
1.5.1.30 homotetramer 4 * 22000, SDS-PAGE Rhodococcus erythropolis

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
1.5.1.30 35
-
enzyme assay Rhodococcus erythropolis
1.14.14.21 35
-
assay at Rhodococcus erythropolis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.30 6
-
enzyme assay Rhodococcus erythropolis
1.14.14.21 7
-
assay at Rhodococcus erythropolis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.5.1.30 6 8.5
-
Rhodococcus erythropolis

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.30 NADH without any chromophore like flavin, NADPH is inert Rhodococcus erythropolis
1.14.14.21 FMNH2
-
Rhodococcus erythropolis
1.14.14.21 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
1.14.14.22 FMNH2
-
Rhodococcus erythropolis
1.14.14.22 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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.5.1.30 0.00338
-
7-hydroxycoumarin
-
Rhodococcus erythropolis

General Information

EC Number General Information Comment Organism
1.14.14.21 metabolism the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1 Rhodococcus erythropolis
1.14.14.21 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
1.14.14.22 metabolism the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1 Rhodococcus erythropolis
1.14.14.22 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