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Literature summary for 1.14.14.22 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Metals/Ions

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

Molecular Weight [Da]

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

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
-

Purification (Commentary)

Purification (Comment) Organism
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]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
807
-
purified enzyme, pH 7.0, 35┬░C 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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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 ?
-
?
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

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

Synonyms

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

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
35
-
-
Rhodococcus erythropolis

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
35
-
purified enzyme, stable up to Rhodococcus erythropolis

pH Optimum

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

pH Stability

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

Cofactor

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

General Information

General Information Comment Organism
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