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
-
desulfurization
- rhodococcus
- erythropolis
- sulfur
- flavin
-
biodesulfurization
-
two-component
- 2-hydroxybiphenyl
-
fossil
- mononucleotide
-
sulfoxidation
- paenibacillus
-
pet28a
-
dszabc
-
hydrodesulfurization
- desulfinase
-
39-fold
-
sulfur-containing
-
flavin-dependent
-
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
ECTree
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Cofactor
Cofactor on EC 1.14.14.21 - dibenzothiophene monooxygenase
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FMNH2
enzyme DszC-FMN crystal structure analysis, FMN-binding site, binding structure and mechanism, modeling, overview
FMNH2
reduced FMN reacts with an oxygen molecule at C4a position of the isoalloxazine ring, producing the C4a-(hydro)peroxyflavin intermediate which is stabilized by residues H391 and S163. H391 may contribute to the formation of the C4a-(hydro)peroxyflavin by acting as a proton donor to the proximal peroxy oxygen, and it might also be involved in the protonation process of C4a-(hydro)peroxyflavin, molecular docking simulation and modeling, overview
FMNH2
the enzyme binds one flavin mononucleotide or reduced flavin mononucleotide (FMNH2) per 90,200-Da homodimer, and FMNH2 is an essential cosubstrate for its activity
NADH
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DszD is responsible for supplying reducing equivalents in the form of FMNH2 to the monooxygenase DszC
NADH
the enzyme does not directly react with NADH, but uses the activity of the FMN:NADH oxidoreductase, DszD
FAD and lumiflavin have only weak activity as reducing agents
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additional information
flavin reductaseFRP is essentially required for enzyme activity providing reduction equivalents, Vibrio harveyi FRP produces FMNH2 at the expense of NADPH and is used to provide FMNH2 for the enzymatic reaction
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additional information
flavin specificity, overview. No activity with FADH2
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additional information
FMN oxidoreductase TdsD, a NADH-dependent FMN oxidoreductase, absolutely required for TdsC activity, maximum activity is obtained at a TdsD/TdsC molar ratio of 0.5, no activity in the absence of TdsD
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additional information
the enzyme requires NADH, FMNH2, oxygen, and the aid of NADH-FMN oxidoreductase to catalyze the conversion of dibenzothiophene
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additional information
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the enzyme requires NADH, FMNH2, oxygen, and the aid of NADH-FMN oxidoreductase to catalyze the conversion of dibenzothiophene
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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
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additional information
the recombinant enzyme is able to utilize either FMNH2 or FADH2 when coupled with a flavin reductase that reduces either FMN or FAD
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