1.14.14.21: dibenzothiophene monooxygenase
This is an abbreviated version!
For detailed information about dibenzothiophene monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.21
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1.14.14.21
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desulfurization
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rhodococcus
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erythropolis
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sulfur
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flavin
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biodesulfurization
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two-component
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2-hydroxybiphenyl
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fossil
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mononucleotide
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sulfoxidation
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paenibacillus
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pet28a
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dszabc
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hydrodesulfurization
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desulfinase
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39-fold
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sulfur-containing
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flavin-dependent
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mesophiles
- 1.14.14.21
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desulfurization
- rhodococcus
- erythropolis
- sulfur
- flavin
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biodesulfurization
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two-component
- 2-hydroxybiphenyl
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fossil
- mononucleotide
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sulfoxidation
- paenibacillus
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pet28a
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dszabc
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hydrodesulfurization
- desulfinase
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39-fold
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sulfur-containing
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flavin-dependent
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mesophiles
Reaction
+ 2 FMNH2 + 2 O2 = + 2 FMN + 2 H2O
Synonyms
BdsC, benzothiophene monooxygenase, BT monooxygenase, cofactor-requiring dibenzothiophene monooxygenase, DBT monooxygenase, DBT-MO, DBT-monooxygenase, dibenzothiophene monooxygenase, dszC, TdsC
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General Information
General Information on EC 1.14.14.21 - dibenzothiophene monooxygenase
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evolution
malfunction
metabolism
physiological function
additional information
DszC with specificity for FMN makes a unique member of the flavin monooxygenase family
evolution
sequence analysis indicates that DszC is similar to the C2 component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii, which can use both FADH2 and FMNH2 as substrates. The monooxygenase components might be divided into three subclasses: the strictly FMNH2-utilizing subclass, the strictly FADH2-utilizing subclass, and the FMNH2 and FADH2 both-utilizing subclass. DszC has the acyl-CoA dehydrogenase folding and experimentally proves to be able to use both FMNH2 and FADH2 as the substrate, therefore, DszC belongs to the FMNH2 and FADH2 both utilizing subclass, phylogenetic analysis of monooxygenase components of the two-component flavin-dependent monooxygenases
evolution
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DszC with specificity for FMN makes a unique member of the flavin monooxygenase family
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evolution
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sequence analysis indicates that DszC is similar to the C2 component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii, which can use both FADH2 and FMNH2 as substrates. The monooxygenase components might be divided into three subclasses: the strictly FMNH2-utilizing subclass, the strictly FADH2-utilizing subclass, and the FMNH2 and FADH2 both-utilizing subclass. DszC has the acyl-CoA dehydrogenase folding and experimentally proves to be able to use both FMNH2 and FADH2 as the substrate, therefore, DszC belongs to the FMNH2 and FADH2 both utilizing subclass, phylogenetic analysis of monooxygenase components of the two-component flavin-dependent monooxygenases
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site-directed mutagenesis study shows that mutations in the residues involved either in catalysis or in flavin or substrate-binding result in a complete loss of enzyme activity, suggesting that the accurate positions of flavin and substrate are crucial for the enzyme activity
malfunction
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site-directed mutagenesis study shows that mutations in the residues involved either in catalysis or in flavin or substrate-binding result in a complete loss of enzyme activity, suggesting that the accurate positions of flavin and substrate are crucial for the enzyme activity
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DBT monooxygenase from Rhodococcus erythropolis is involved in the first step of the 4S pathway. Dibenzothiophene and its derivatives are resistant to the hydrodesulfurization method often used in industry, but they are susceptible to enzymatic desulfurization via the 4S pathway
metabolism
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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 stoichiometric due to the volatile nature of 2'-hydroxybiphenyl-2-sulfinate
metabolism
dibenzothiophene monooxygenase is the first enzyme involved in the degradation of dibenzothiophene
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 DBT monooxygenase from Rhodococcus erythropolis D-1 is involved in the first two steps of the 4S pathway. The 4S metabolic pathway catalyzes the sequential conversion of DBT to 2'-hydroxybiphenyl via three enzymes encoded by the dsz operon in several bacterial species
metabolism
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the dibenzothiophene (DBT) desulfurization enzyme system consists of three enzymes: DBT monooxygenase, DBT sulfone monooxygenase, and 2'-hydroxybiphenyl 2-sulfinate desulfinase
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
Gordonia sp. F.5.25.8
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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 stoichiometric due to the volatile nature of 2'-hydroxybiphenyl-2-sulfinate
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metabolism
Rhodococcus erythropolis IGTS8 / ATCC 53968
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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
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metabolism
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the dibenzothiophene (DBT) desulfurization enzyme system consists of three enzymes: DBT monooxygenase, DBT sulfone monooxygenase, and 2'-hydroxybiphenyl 2-sulfinate desulfinase
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metabolism
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dibenzothiophene monooxygenase is the first enzyme involved in the degradation of dibenzothiophene
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metabolism
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the enzyme is involved in the dibenzothiophene desulfurization pathway of Rhodococcus erythropolis strain D-1
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metabolism
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the enzyme is involved in the dibenzothiophene desulfurizing metabolizing dibenzothiophene to form 2-hydroxybiphenyl without breaking the carbon skeleton, dibenzothiophene desulfurization pathway, overview
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metabolism
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the DBT monooxygenase from Rhodococcus erythropolis D-1 is involved in the first two steps of the 4S pathway. The 4S metabolic pathway catalyzes the sequential conversion of DBT to 2'-hydroxybiphenyl via three enzymes encoded by the dsz operon in several bacterial species
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metabolism
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the enzyme is involved in the pathway of microbial dibenzothiophene desulfurization, overview
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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
flavin reductase or flavin-dependent monooxygenase efficiently couples with the other component in two-component monooxygenases. Coexpression of frb with the DBT-desulfurization genes (bdsABC) from Bacillus subtilis strain WU-S2B is critical for high DBT-desulfurizing ability over a wide temperature range of 20-55°C
physiological function
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Mycobacterium phlei strain GTIS10 converts dibenzothiophene to 2'-hydroxybiphenyl, determination of metabolites from dibenzothiophene, overview
physiological function
the dibenzothiophene (DBT) monooxygenase DszC, which is the key initiating enzyme in 4S metabolic pathway, catalyzes sequential sulphoxidation reaction of DBT to DBT sulfoxide (DBTO), then DBT sulfone (DBTO2). Residues H391, and D392 directly participate in catalysis. Residues H92, Y96, N129, F161, S163, W205, R282, R370, and H388 are involved in flavin or substrate-binding
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
Mycolicibacterium phlei GTIS10
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Mycobacterium phlei strain GTIS10 converts dibenzothiophene to 2'-hydroxybiphenyl, determination of metabolites from dibenzothiophene, overview
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physiological function
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the dibenzothiophene (DBT) monooxygenase DszC, which is the key initiating enzyme in 4S metabolic pathway, catalyzes sequential sulphoxidation reaction of DBT to DBT sulfoxide (DBTO), then DBT sulfone (DBTO2). Residues H391, and D392 directly participate in catalysis. Residues H92, Y96, N129, F161, S163, W205, R282, R370, and H388 are involved in flavin or substrate-binding
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physiological function
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flavin reductase or flavin-dependent monooxygenase efficiently couples with the other component in two-component monooxygenases. Coexpression of frb with the DBT-desulfurization genes (bdsABC) from Bacillus subtilis strain WU-S2B is critical for high DBT-desulfurizing ability over a wide temperature range of 20-55°C
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physiological function
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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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physiological function
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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
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C-terminal DBT-binding site by using a molecular docking simulation that simultaneously docks the FMN cofactor and DBT substrate to an apo-DszC structure, role of the C terminus in catalysis
additional information
flavin reductase (DszD) is essential for the enzyme activity of DszC
additional information
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the C-terminus (410-417) of enzyme DszC, which is located in the interior of the protein, is important for the stabilization of the active conformation of the substrate-binding pocket and the tetrameric state and plays a significant role in the catalytic activity of the enzyme. The residues around the site are conserved: Tyr96, Asn129, Phe161, Ser163, Trp205, Ser215, Phe250, and His391
additional information
two distinct conformations occur in the flexible lid loops adjacent to the active site (residue 280-295, between helix alpha9 and alpha10), that are named open and closed state, respectively, and might show the status of the free and ligand-bound DszC
additional information
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two distinct conformations occur in the flexible lid loops adjacent to the active site (residue 280-295, between helix alpha9 and alpha10), that are named open and closed state, respectively, and might show the status of the free and ligand-bound DszC
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additional information
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flavin reductase (DszD) is essential for the enzyme activity of DszC
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additional information
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C-terminal DBT-binding site by using a molecular docking simulation that simultaneously docks the FMN cofactor and DBT substrate to an apo-DszC structure, role of the C terminus in catalysis
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