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Literature summary for 1.14.14.22 extracted from

  • Ohshiro, T.; Izumi, Y.
    Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization (2000), Bioseparation, 9, 185-188.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information flavin reductase (DszD) is essential for the enzyme activity of DszA 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 from strain D-1 by ammonium sulfate fractionation, two different steps of anion exchange chromatography, hydrophobic interaction chromatography, 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. Interaction with purified flavin reductase from the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, with DszA 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. Interaction with purified flavin reductase from the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, with DszA 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
-
assay at Rhodococcus erythropolis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
FMNH2
-
Rhodococcus erythropolis

General Information

General Information Comment Organism
additional information flavin reductase (DszD) is essential for the enzyme activity of DszA Rhodococcus erythropolis