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metabolism

-
the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1
metabolism
-
the enzyme is involved in the dibenzothiophene desulfurizing metabolizing dibenzothiophene to form 2-hydroxybiphenyl without breaking the carbon skeleton, dibenzothiophene desulfurization pathway, overview
metabolism
-
dibenzothiophene is converted to 2'-hydroxybiphenyl-2-sulfinate by ec1.14.14.21 and 1.14.14.22 in strain F.5.25.8, and the 2'-hydroxybiphenyl-2-sulfinate concentration does not decrease during the stationary phase. Although the production of 2'-hydroxybiphenyl-2-sulfinate appears to proceed in parallel with the increase in biomass, the relationship between the decrease in dibenzothiophene and increase in 2'-hydroxybiphenyl-2-sulfinate does not seem stoichiometricdue to the volatile nature of 2'-hydroxybiphenyl-2-sulfinate
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
metabolism
-
the enzyme is involved in the pathway of microbial dibenzothiophene desulfurization, overview
metabolism
-
strain IGTS8 has the ability to convert dibenzothiophene to 2-hydroxybiphenyl with the release of inorganic sulfur. The conversion of dibenzothiophene to 2-hydroxybiphenyl is catalyzed by a multienzyme pathway consisting of two monooxygenases and a desulfinase. The final reaction catalyzed by the desulfinase DszB appears to be the rate limiting step in the pathway
metabolism
-
dibenzothiophene is converted to 2'-hydroxybiphenyl-2-sulfinate by ec1.14.14.21 and 1.14.14.22 in strain F.5.25.8, and the 2'-hydroxybiphenyl-2-sulfinate concentration does not decrease during the stationary phase. Although the production of 2'-hydroxybiphenyl-2-sulfinate appears to proceed in parallel with the increase in biomass, the relationship between the decrease in dibenzothiophene and increase in 2'-hydroxybiphenyl-2-sulfinate does not seem stoichiometricdue to the volatile nature of 2'-hydroxybiphenyl-2-sulfinate
-
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; the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1; the enzyme is involved in the dibenzothiophene desulfurizing metabolizing dibenzothiophene to form 2-hydroxybiphenyl without breaking the carbon skeleton, dibenzothiophene desulfurization pathway, overview; the enzyme is involved in the pathway of microbial dibenzothiophene desulfurization, overview
-
metabolism
-
strain IGTS8 has the ability to convert dibenzothiophene to 2-hydroxybiphenyl with the release of inorganic sulfur. The conversion of dibenzothiophene to 2-hydroxybiphenyl is catalyzed by a multienzyme pathway consisting of two monooxygenases and a desulfinase. The final reaction catalyzed by the desulfinase DszB appears to be the rate limiting step in the pathway
-
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
physiological function
-
DszC and DszA catalyze monooxygenation reactions in the desulfurization of dibenzothiophene, both requiring the additional enzyme flavin reductase, which catalyzes the reduction of flavin by NAD(P)H to form reduced flavin
physiological function
-
Mycobacterium phlei strain GTIS10 converts dibenzothiophene to 2'-hydroxybiphenyl, determination of metabolites from dibenzothiophene, overview
physiological function
-
Mycobacterium phlei strain GTIS10 converts dibenzothiophene to 2'-hydroxybiphenyl, determination of metabolites from dibenzothiophene, overview
-
physiological function
-
DszC and DszA catalyze monooxygenation reactions in the desulfurization of dibenzothiophene, both requiring the additional enzyme flavin reductase, which catalyzes the reduction of flavin by NAD(P)H to form reduced flavin; 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
-
additional information

-
flavin reductase (DszD) is essential for the enzyme activity of DszA
additional information
-
residue Q345 is involved in C-S bond cleavage specifically for alkylated dibenzothiophene sulfone
additional information
-
flavin reductase (DszD) is essential for the enzyme activity of DszA
-
additional information
-
residue Q345 is involved in C-S bond cleavage specifically for alkylated dibenzothiophene sulfone
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
2-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
3,4,6-trimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
3,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
3-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
-
-
-
-
?
3-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
? + 2 FMN + H2O
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
-
-
-
-
?
4-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
dibenz[c,e][1,2] oxathiin 6-oxide + 2 FMNH2 + O2
2,2'-dihydroxybiphenyl + 2 FMN + H2O
dibenz[c,e][1,2]oxathiin 6,6-dioxide + 2 FMNH2 + O2
2,2'-dihydroxybiphenyl + 2 FMN + H2O
additional information
?
-
1-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2

?
-
-
-
-
?
1-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
-
-
-
-
?
2-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2

?
-
-
-
-
?
2-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
-
-
-
-
?
3,4,6-trimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2

?
-
-
-
-
?
3,4,6-trimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
-
-
-
-
?
3,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2

?
-
-
-
-
?
3,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
-
-
-
-
?
3-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2

? + 2 FMN + H2O
-
activity of mutant Q345A
-
-
?
3-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
? + 2 FMN + H2O
-
activity of mutant Q345A
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2

2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
best substrate
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
best substrate
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenz[c,e][1,2] oxathiin 6-oxide + 2 FMNH2 + O2

2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
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
-
-
?
dibenz[c,e][1,2] oxathiin 6-oxide + 2 FMNH2 + O2
2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
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
-
-
?
dibenz[c,e][1,2]oxathiin 6,6-dioxide + 2 FMNH2 + O2

2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
i.e. sultone
-
-
?
dibenz[c,e][1,2]oxathiin 6,6-dioxide + 2 FMNH2 + O2
2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
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
-
-
?
dibenz[c,e][1,2]oxathiin 6,6-dioxide + 2 FMNH2 + O2
2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
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
-
-
?
dibenz[c,e][1,2]oxathiin 6,6-dioxide + 2 FMNH2 + O2
2,2'-dihydroxybiphenyl + 2 FMN + H2O
-
i.e. sultone
-
-
?
additional information

?
-
-
coupled reaction with flavin reductase (TdsD) from thermophilic Paenibacillus sp. strain A11-2
-
-
-
additional information
?
-
-
The dszA gene encodes DBT-5,5-dioxide monooxygenase, which catalyzes the conversion of dibenzothiophene sulfone to 2'-hydroxybiphenyl-2-sulfinate
-
-
-
additional information
?
-
-
The dszA gene encodes DBT-5,5-dioxide monooxygenase, which catalyzes the conversion of dibenzothiophene sulfone to 2'-hydroxybiphenyl-2-sulfinate
-
-
-
additional information
?
-
-
FMN:NADPH oxidoreductase from Vibrio harveyi complements activities of purified DszA and DszC proteins. DszA and DszC are oxygenase units that do not use NAD(P)H directly, but instead use FMNH2 from a FMN:NADPH oxidoreductase for oxygenation. The oxygenase and oxidoreductase units do not interact but exchange electrons, overview. Purified DszC or DszA proteins exhibit no activity in presence of 10 mM FMN, 5 mM NADPH, oxygen, and organosulfur substrates
-
-
-
additional information
?
-
-
analysis of the coupled reaction of DszA with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview
-
-
-
additional information
?
-
-
no activity with 4,6-dibutyldibenzothiophene sulfone by wild-type and mutant enzymes
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
no activity with dibenzothiophene and 2'-hydroxybiphenyl 2-sulfinic acid. DszA may recognize the sulfone moiety within the structure of DBT sulfone and sultone
-
-
-
additional information
?
-
-
analysis of the coupled reaction of DszA with the purified NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1, overview
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
no activity with dibenzothiophene and 2'-hydroxybiphenyl 2-sulfinic acid. DszA may recognize the sulfone moiety within the structure of DBT sulfone and sultone
-
-
-
additional information
?
-
-
FMN:NADPH oxidoreductase from Vibrio harveyi complements activities of purified DszA and DszC proteins. DszA and DszC are oxygenase units that do not use NAD(P)H directly, but instead use FMNH2 from a FMN:NADPH oxidoreductase for oxygenation. The oxygenase and oxidoreductase units do not interact but exchange electrons, overview. Purified DszC or DszA proteins exhibit no activity in presence of 10 mM FMN, 5 mM NADPH, oxygen, and organosulfur substrates
-
-
-
additional information
?
-
-
no activity with 4,6-dibutyldibenzothiophene sulfone by wild-type and mutant enzymes
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
additional information
?
-
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2

2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
Q9LBX4
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
Q9LBX4
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
Q6WE15
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
Q6WE15
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
U3GQJ5
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
U3GQJ5
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
?
additional information

?
-
-
The dszA gene encodes DBT-5,5-dioxide monooxygenase, which catalyzes the conversion of dibenzothiophene sulfone to 2'-hydroxybiphenyl-2-sulfinate
-
-
-
additional information
?
-
-
The dszA gene encodes DBT-5,5-dioxide monooxygenase, which catalyzes the conversion of dibenzothiophene sulfone to 2'-hydroxybiphenyl-2-sulfinate
-
-
-
additional information
?
-
-
FMN:NADPH oxidoreductase from Vibrio harveyi complements activities of purified DszA and DszC proteins. DszA and DszC are oxygenase units that do not use NAD(P)H directly, but instead use FMNH2 from a FMN:NADPH oxidoreductase for oxygenation. The oxygenase and oxidoreductase units do not interact but exchange electrons, overview. Purified DszC or DszA proteins exhibit no activity in presence of 10 mM FMN, 5 mM NADPH, oxygen, and organosulfur substrates
-
-
-
additional information
?
-
-
FMN:NADPH oxidoreductase from Vibrio harveyi complements activities of purified DszA and DszC proteins. DszA and DszC are oxygenase units that do not use NAD(P)H directly, but instead use FMNH2 from a FMN:NADPH oxidoreductase for oxygenation. The oxygenase and oxidoreductase units do not interact but exchange electrons, overview. Purified DszC or DszA proteins exhibit no activity in presence of 10 mM FMN, 5 mM NADPH, oxygen, and organosulfur substrates
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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6
-
purified enzyme, pH 7.0, 50°C, substrate 3,6-dimethyldibenzothiophene-5,5-dioxide
12.4
-
purified enzyme, pH 7.0, 50°C, substrate 4-methyldibenzothiophene-5,5-dioxide
22.4
-
purified enzyme, pH 7.0, 50°C, substrate 1-methyldibenzothiophene-5,5-dioxide
29.6
-
purified enzyme, pH 7.0, 50°C, substrate 3-methyldibenzothiophene-5,5-dioxide
37.2 - 40
-
purified enzyme, pH 7.0, 50°C, substrate dibenzothiophene-5,5-dioxide
38.4
-
purified enzyme, pH 7.0, 50°C, substrate 2-methyldibenzothiophene-5,5-dioxide
62.4
-
purified enzyme, pH 7.0, 50°C, substrate 3,4,6-trimethyldibenzothiophene-5,5-dioxide
77.2
-
purified enzyme, pH 7.0, 50°C, substrate 4,6-dimethyldibenzothiophene-5,5-dioxide
807
-
purified enzyme, pH 7.0, 35°C
855
-
purified native enzyme, pH 7.0, 50°C
875
-
purified recombinant enzyme, pH 7.0, 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Matsubara, T.; Ohshiro, T.; Nishina, Y.; Izumi, Y.
Purification, characterization, and overexpression of flavin reductase involved in dibenzothiophene desulfurization by Rhodococcus erythropolis D-1
Appl. Environ. Microbiol.
67
1179-1184
2001
Rhodococcus erythropolis (Q6WE15), Rhodococcus erythropolis D-1 (Q6WE15)
brenda
Ohshiro, T.; Aoi, Y.; Torii, K.; Izumi, Y.
Flavin reductase coupling with two monooxygenases involved in dibenzothiophene desulfurization: purification and characterization from a non-desulfurizing bacterium, Paenibacillus polymyxa A-1
Appl. Microbiol. Biotechnol.
59
649-657
2002
Rhodococcus erythropolis (Q6WE15), Rhodococcus erythropolis D-1 (Q6WE15)
brenda
Kayser, K.J.; Cleveland, L.; Park, H.S.; Kwak, J.H.; Kolhatkar, A.; Kilbane, J.J.
Isolation and characterization of a moderate thermophile, Mycobacterium phlei GTIS10, capable of dibenzothiophene desulfurization
Appl. Microbiol. Biotechnol.
59
737-745
2002
Mycobacterium phlei, Mycobacterium phlei GTIS10
brenda
Santos, S.C.; Alviano, D.S.; Alviano, C.S.; Padula, M.; Leitao, A.C.; Martins, O.B.; Ribeiro, C.M.; Sassaki, M.Y.; Matta, C.P.; Bevilaqua, J.; Sebastian, G.V.; Seldin, L.
Characterization of Gordonia sp. strain F.5.25.8 capable of dibenzothiophene desulfurization and carbazole utilization
Appl. Microbiol. Biotechnol.
71
355-362
2006
Gordonia sp., Gordonia sp. F.5.25.8
brenda
Xi, L.; Squires, C.H.; Monticello, D.J.; Childs, J.D.
A flavin reductase stimulates DszA and DszC proteins of Rhodococcus erythropolis IGTS8 in vitro
Biochem. Biophys. Res. Commun.
230
73-75
1997
Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 / ATCC 53968
brenda
Ishii, Y.; Konishi, J.; Okada, H.; Hirasawa, K.; Onaka, T.; Suzuki, M.
Operon structure and functional analysis of the genes encoding thermophilic desulfurizing enzymes of Paenibacillus sp. A11-2
Biochem. Biophys. Res. Commun.
270
81-88
2000
Paenibacillus sp. (Q9LBX4), Paenibacillus sp. A11-2 (Q9LBX4)
brenda
Li, G.Q.; Ma, T.; Li, S.S.; Li, H.; Liang, F.L.; Liu, R.L.
Improvement of dibenzothiophene desulfurization activity by removing the gene overlap in the dsz operon
Biosci. Biotechnol. Biochem.
71
849-854
2007
Rhodococcus erythropolis (Q6WE15), Rhodococcus erythropolis D-1 (Q6WE15)
brenda
Ohshiro, T.; Izumi, Y.
Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization
Bioseparation
9
185-188
2000
Rhodococcus erythropolis (Q6WE15), Rhodococcus erythropolis D-1 (Q6WE15)
brenda
Konishi, J.; Maruhashi, K.
Residue 345 of dibenzothiophene (DBT) sulfone monooxygenase is involved in C-S bond cleavage specificity of alkylated DBT sulfones
Biotechnol. Lett.
25
1199-1202
2003
Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 / ATCC 53968
brenda
Akhtar, N.; Ghauri, M.; Anwar, M.; Heaphy, S.
Phylogenetic characterization and novelty of organic sulphur metabolizing genes of Rhodococcus spp. (Eu-32)
Biotechnol. Lett.
37
837-847
2015
Rhodococcus sp. (U3GQJ5), Rhodococcus sp. Eu-32 (U3GQJ5)
-
brenda
Kobayashi, M.; Onaka, T.; Ishii, Y.; Konishi, J.; Takaki, M.; Okada, H.; Ohta, Y.; Koizumi, K.; Suzuki, M.
Desulfurization of alkylated forms of both dibenzothiophene and benzothiophene by a single bacterial strain
FEMS Microbiol. Lett.
187
123-126
2000
Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 / ATCC 53968
brenda
Mohamed, M.El-S.; Al-Yacoub, Z.H.; Vedakumar, J.V.
Biocatalytic desulfurization of thiophenic compounds and crude oil by newly isolated bacteria
Front. Microbiol.
6
112
2015
Rhodococcus sp., Stenotrophomonas sp.
brenda
Ohshiro, T.; Ishii, Y.; Matsubara, T.; Ueda, K.; Izumi, Y.; Kino, K.; Kirimura, K.
Dibenzothiophene desulfurizing enzymes from moderately thermophilic bacterium Bacillus subtilis WU-S2B: purification, characterization and overexpression
J. Biosci. Bioeng.
100
266-273
2005
Bacillus subtilis, Bacillus subtilis WU-S2B
brenda
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
J. Biosci. Bioeng.
88
610-616
1999
Rhodococcus erythropolis (Q6WE15), Rhodococcus erythropolis, Rhodococcus erythropolis D-1 (Q6WE15)
brenda
Konishi, J.; Ishii, Y.; Onaka, T.; Ohta, Y.; Suzuki, M.; Maruhashi, K.
Purification and characterization of dibenzothiophene sulfone monooxygenase and FMN-dependent NADH oxidoreductase from the thermophilic bacterium Paenibacillus sp. strain A11-2
J. Biosci. Bioeng.
90
607-613
2000
Paenibacillus sp., Paenibacillus sp. (Q9LBX4), Paenibacillus sp. A11-2 (Q9LBX4)
brenda
Izumi, Y.; Ohshiro, T.
Purification and characterization of enzymes involved in desulfurization of dibezothiophene in fossil fuels
J. Mol. Catal. B
11
1061-1064
2001
Rhodococcus erythropolis (Q6WE15), Rhodococcus erythropolis D-1 (Q6WE15)
-
brenda
Gray, K.A.; Pogrebinsky, O.S.; Mrachko, G.T.; Xi, L.; Monticello, D.J.; Squires, C.H.
Molecular mechanisms of biocatalytic desulfurization of fossil fuels
Nat. Biotechnol.
14
1705-1709
1996
Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 / ATCC 53968
brenda