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Enzyme Nomenclature
Information on EC 1.14.14.22 - dibenzothiophene sulfone monooxygenase
for references in articles please use BRENDA:EC1.14.14.22
Word Map on EC 1.14.14.22
- 1.14.14.22
-
desulfurization
-
rhodococcus
- erythropolis
- sulfur
- 2-hydroxybiphenyl
- desulfinase
- subtilis
-
mesophilic
- paenibacillus
- flavin
-
biodesulfurization
-
petroleum
-
carbon-sulfur
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.14.22
-
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RECOMMENDED NAME
GeneOntology No.
dibenzothiophene sulfone monooxygenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2 = 2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
dibenzothiophene-5,5-dioxide,FMNH2:oxygen oxidoreductase
This bacterial enzyme catalyses a step in the desulfurization pathway of dibenzothiophenes. The enzyme forms a two-component system with a dedicated NADH-dependent FMN reductase (EC 1.5.1.42) encoded by the dszD gene, which also interacts with EC 1.14.14.21, dibenzothiophene monooxygenase.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
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
Gordonia sp. F.5.25.8
-
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
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
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
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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
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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
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
residue Q345 is involved in C-S bond cleavage specifically for alkylated dibenzothiophene sulfone
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4,6-trimethyldibenzothiophene-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
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
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
Gordonia sp. F.5.25.8
-
-
-
-
?
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
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
-
-
-
?
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
?
-
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
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
?
-
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
no activity with 4,6-dibutyldibenzothiophene sulfone by wild-type and mutant enzymes
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Gordonia sp. F.5.25.8
-
-
-
-
?
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
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
-
-
-
?
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
?
-
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
the enzyme does not directly react with NADH, but uses the activity of the FMN:NADH oxidoreductase, DszD
additional information
-
the flavin reductase, EC 1.5.1.36, from Rhodococcus erythropolis strain D-1 grown in a medium containing dibenzothiophene as the sole source of sulfur is essential for the reactions of the two monooxygenases DszC and DszA in vivo. The purified flavin reductase contains no chromogenic cofactors and has a molecular mass of 86 kDa and four identical 22-kDa subunits. The enzyme catalyzes NADH-dependent reduction of flavin mononucleotide, FMN. The flavin reductase does not catalyze reduction of any nitroaromatic compound
-
additional information
-
NADH flavin reductase, essentially required
-
additional information
-
the purified TdsA absolutely requires an oxidoreductase for its activity, oxidoreductase TdsD is completely FMN-dependent, and FAD does not act as a cofactor. TsdD is active with NADH and NADPH to the same extent. TdsA exhibits no activity in the absence of TdsD
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no or poor effect by 1 mM of Al3+, Zn2+, Mg2+, semicarbazide, and NaF
additional information
-
the enzyme does not contain Fe2+ or Zn2+, no stimulation by Fe3+, Fe2+, or Cu2+, enzyme DszA does not require a metal cofactor
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
NADPH-preferring flavin reductase from Paenibacillus polymyxa A-1 increases the catalytic activity of enzyme DszA 5fold compared to the activity with Rhodococcus erythropolis strain D-1 flavin reductase. The flavin reuctase from Vibrio harveyi is also stimulating. In the microbial DBT-desulfurization, flavin reductase from the non-DBT-desulfurizing bacterium is superior to that from the DBT-desulfurizing bacterium
-
additional information
-
flavin reductase (DszD) is essential for the enzyme activity of DszA
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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the organism can use dibenzothiophene as a sole source of sulfur for growth at 30-52°C, it can also utilize benzothiophene and thiophene as sulfur sources for growth. Range of organosulfur substrates utilized as a sole source of sulfur for growth by Mycobacterium phlei GTIS10, best is dibenzothiophene, overview
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the organism can use dibenzothiophene as a sole source of sulfur for growth at 30-52°C, it can also utilize benzothiophene and thiophene as sulfur sources for growth. Range of organosulfur substrates utilized as a sole source of sulfur for growth by Mycobacterium phlei GTIS10, best is dibenzothiophene, overview
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additional information
-
the strain is enriched from oil contaminated soil, in presence of dibenzothiophene as the sole sulfur source
additional information
-
the strain is enriched from oil contaminated soil, in presence of dibenzothiophene as the sole sulfur source
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
homodimer
-
2 * 50000, SDS-PAGE; 2 * 50000, SDS-PAGE; 2 * 50000, SDS-PAGE
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme DszA, hanging drop vapour diffusion method, using a reservoir suliton containing 12% polyethylene glycol 400 and 0.2 M CaCl2, 4°C, X-ray diffraction structure determination and analysis
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 102fold to homogeneity by two different steps of anion exchange chromatography, followed by hydrophobic interaction chromatography, and gel filtration
-
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
-
native enzyme 47.6fold by anion exchange and hydrophobic interaction chromatography, followed by another different step of anion exchange chromatography and hydroxyapatite chromatography
-
native enzyme 82.6fold from strain WU-S2B by three different steps of anion exchange chromatography and one step of hydrophobic interaction chromatography, gel filtration, and another step of anion exchange chromatography, recombinant enzyme from Escherichia coli 17.0fold to homogeneity by anion exchange and hydrophobic interaction chromatography, and again anion exchange chromatography
-
native enzyme from strain IGTS8 by anion exchange chromatography and gel filtration
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native enzyme to homogeneity by anion exchange and hydrophobic interaction chromatography, and gel filtration
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recombinant His-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinty chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene bdsA, recombinant overexpression in Escherichia coli, coexpression with chaperone groEL/groES genes
-
gene dszA
gene dszA, cloning from dszABC operon, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis
gene dszA, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression of His-tagged enzyme in Escherichia coli strain DH5alpha
-
gene dszA, DNA and amino acid sequence determination and analysis, sequence comparisons
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gene dszA, recombinant expression of the complete dszABC operon, revealing that the ratio of mRNA quantity of dszA, dszB, and dszC is 11:3.3:1, the expression level of dszB is far lower than that of dszC. The termination codon of dszA and the initiation codon of dszB overlap, whereas there is a 13-bp gap between genes dszB and dszC. Quantitative analysis of dsz operon transcription by real-time PCR
gene dszA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain JM109
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gene tdsA, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli, coexpression with genes tdsC and tdsB, leading to established thermophilic desulfurization of dibenzothiophene in Escherichia coli host, an Escherichia coli oxidoreductase can be functionally coupled with the monooxygenases of a gram-positive thermophile. The end of tdsA shows a 4-bp overlap with the translational start site of tdsB
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L346A
-
site-directed mutagenesis, the mutant shows an unaltered substrate specificity compared to the wild-type enzyme
Q345A
-
site-directed mutagenesis, the mutant strain can degrade octyl sulfide on which the wild-type strain cannot grow. the DszA change at residue 345 results in an altered C-S bond cleavage pattern of 3-methyl DBT sulfone
T344A
-
site-directed mutagenesis, the mutant shows an unaltered substrate specificity compared to the wild-type enzyme
T344A/Q345A
-
site-directed mutagenesis, the mutant strain can degrade octyl sulfide on which the wild-type strain cannot grow. the DszA change at residue 345 results in an altered C-S bond cleavage pattern of 3-methyl DBT sulfone
L346A
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
site-directed mutagenesis, the mutant shows an unaltered substrate specificity compared to the wild-type enzyme
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Q345A
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
site-directed mutagenesis, the mutant strain can degrade octyl sulfide on which the wild-type strain cannot grow. the DszA change at residue 345 results in an altered C-S bond cleavage pattern of 3-methyl DBT sulfone
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T344A
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
site-directed mutagenesis, the mutant shows an unaltered substrate specificity compared to the wild-type enzyme
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T344A/Q345A
Rhodococcus erythropolis IGTS8 / ATCC 53968
-
site-directed mutagenesis, the mutant strain can degrade octyl sulfide on which the wild-type strain cannot grow. the DszA change at residue 345 results in an altered C-S bond cleavage pattern of 3-methyl DBT sulfone
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additional information
additional information
removal of the 13-bp gap between genes dszB and dszC from the dszABC operon of wild-type strain D-1 results in a 5fold increased desulfurization activity of resting Rhodococcus erythropolis cells with redesigned dsc operon, termed strain D-2
additional information
-
removal of the 13-bp gap between genes dszB and dszC from the dszABC operon of wild-type strain D-1 results in a 5fold increased desulfurization activity of resting Rhodococcus erythropolis cells with redesigned dsc operon, termed strain D-2
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
TdsA shows higher activity toward bulkier substrates than its mesophilic counterpart, DszA. These properties suggest the applicability of biodesulfmizatfon to the processing of actual petroleum fractions
additional information
-
TdsA shows higher activity toward bulkier substrates than its mesophilic counterpart, DszA. These properties suggest the applicability of biodesulfmizatfon to the processing of actual petroleum fractions
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.14.22)
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