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Literature summary extracted from

  • Ohshiro, T.; Kojima, T.; Torii, K.; Kawasoe, H.; Izumi, Y.
    Purification and characterization of dibenzothiophene (DBT) sulfone monooxygenase, an enzyme involved in DBT desulfurization, from Rhodococcus erythropolis D-1 (1999), J. Biosci. Bioeng., 88, 610-616.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.22 gene dszA, DNA and amino acid sequence determination and analysis, sequence comparisons Rhodococcus erythropolis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.22 purified enzyme, 4°C, hanging drop vapor diffusion method, mixing of 42 mg/ml protein in 1 mM Tris-HCl buffer, pH 8.0, with an equal volume of well solution containing 12% PEG 400, 0.2 M CaCl*, and 0.01 M HEPES buffer, pH 7.5, 1 week, X-ray diffraction structure determination and analysis Rhodococcus erythropolis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.22 1,10-phenanthroline 37% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 2,2'-bipyridine
-
Rhodococcus erythropolis
1.14.14.22 2,2-bipyridine 62% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 8-Quinolinol 88% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 Ca2+ 81% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 Co2+ 27% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 Cu2+ complete inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 EDTA 49% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 Fe2+ 32% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 Hg2+ complete inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 Li+ 20% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 Mn2+ 72% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 N-bromosuccinimide 17% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 N-ethylmaleimide 27% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 Ni2+ 78% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 NO3- 39% inhibition at 1 mM Rhodococcus erythropolis
1.14.14.22 p-chloromercuribenzoic acid 50% inhibition at 1 mM Rhodococcus erythropolis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.22 5,5'-dithiobis(2-nitrobenzoic acid) slightly activating at 0.1 mM Rhodococcus erythropolis
1.14.14.22 Cd2+ slightly activating at 1 mM Rhodococcus erythropolis
1.14.14.22 additional information no or poor effect by 1 mM of Al3+, Zn2+, Mg2+, semicarbazide, and NaF Rhodococcus erythropolis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.22 50000
-
2 * 50000, SDS-PAGE Rhodococcus erythropolis
1.14.14.22 97000
-
gel filtration Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.22 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
1.14.14.22 Rhodococcus erythropolis Q6WE15 gene dszA
-
1.14.14.22 Rhodococcus erythropolis D-1 Q6WE15 gene dszA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.22 native enzyme 102fold to homogeneity by two different steps of anion exchange chromatography, followed by hydrophobic interaction chromatography, and gel filtration Rhodococcus erythropolis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.14.22 807
-
purified enzyme, pH 7.0, 35°C Rhodococcus erythropolis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 dibenz[c,e][1,2] oxathiin 6-oxide + 2 FMNH2 + O2 i.e. sultine, sultine is nonenzymatically hydrolyzed to form 2'-hydroxybiphenyl 2-sulfinic acid, it is also oxidized to sultone. Once sultone is nonenzymatically formed from sultine, it is immediately converted to 2,2'-dihydroxybiphenyl by DszA Rhodococcus erythropolis 2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
?
1.14.14.22 dibenz[c,e][1,2] oxathiin 6-oxide + 2 FMNH2 + O2 i.e. sultine, sultine is nonenzymatically hydrolyzed to form 2'-hydroxybiphenyl 2-sulfinic acid, it is also oxidized to sultone. Once sultone is nonenzymatically formed from sultine, it is immediately converted to 2,2'-dihydroxybiphenyl by DszA Rhodococcus erythropolis D-1 2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
?
1.14.14.22 dibenz[c,e][1,2]oxathiin 6,6-dioxide + 2 FMNH2 + O2 i.e. sultone, sultine is nonenzymatically hydrolyzed to form 2'-hydroxybiphenyl 2-sulfinic acid, it is also oxidized to sultone. Once sultone is nonenzymatically formed from sultine, it is immediately converted to 2,2'-dihydroxybiphenyl by DszA Rhodococcus erythropolis 2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
?
1.14.14.22 dibenz[c,e][1,2]oxathiin 6,6-dioxide + 2 FMNH2 + O2 i.e. sultone, sultine is nonenzymatically hydrolyzed to form 2'-hydroxybiphenyl 2-sulfinic acid, it is also oxidized to sultone. Once sultone is nonenzymatically formed from sultine, it is immediately converted to 2,2'-dihydroxybiphenyl by DszA Rhodococcus erythropolis D-1 2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
?
1.14.14.22 additional information no activity with dibenzothiophene and 2'-hydroxybiphenyl 2-sulfinic acid, substrate specificity, overview. DszA may recognize the sulfone moiety within the structure of DBT sulfone and sultone Rhodococcus erythropolis ?
-
?
1.14.14.22 additional information no activity with dibenzothiophene and 2'-hydroxybiphenyl 2-sulfinic acid, substrate specificity, overview. DszA may recognize the sulfone moiety within the structure of DBT sulfone and sultone Rhodococcus erythropolis D-1 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.14.14.22 homodimer 2 * 50000, SDS-PAGE Rhodococcus erythropolis

Synonyms

EC Number Synonyms Comment Organism
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
1.14.14.22 35
-
-
Rhodococcus erythropolis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.14.14.22 35
-
purified enzyme, stable up to Rhodococcus erythropolis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.22 7.5
-
-
Rhodococcus erythropolis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.14.14.22 6 10 purified enzyme, stable at Rhodococcus erythropolis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.22 FMNH2 essentially required Rhodococcus erythropolis
1.14.14.22 additional information NADH flavin reductase, essentially required Rhodococcus erythropolis

General Information

EC Number General Information Comment Organism
1.14.14.22 metabolism enzyme DszA is involved in the microbial DBT desulfurization metabolism and catalyzes the conversion of dibenzothiophene sulfone to 2'-hydroxybiphenyl 2-sulfinic acid in the presence of flavin reductase with cleavage of the carbon-sulfur bond in the dibenzothiophene skeleton Rhodococcus erythropolis