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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
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-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, 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
-
-
?
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
-
-
?
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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
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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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
-
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
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
the enzyme is involved in the pathway of microbial dibenzothiophene desulfurization, 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
-
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
-
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
-
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
-
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
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
-
Mycobacterium phlei strain GTIS10 converts dibenzothiophene to 2'-hydroxybiphenyl, determination of metabolites from dibenzothiophene, overview
-
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
-
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
-
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
-
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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.
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Rhodococcus erythropolis, Rhodococcus erythropolis IGTS8 / ATCC 53968
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