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
Synonyms
BdsC, benzothiophene monooxygenase, BT monooxygenase, cofactor-requiring dibenzothiophene monooxygenase, DBT monooxygenase, DBT-MO, DBT-monooxygenase, dibenzothiophene monooxygenase, dszC, TdsC
ECTree
1.14.14.21 dibenzothiophene monooxygenaseAdvanced search results
results (
results (Subunits
Subunits on EC 1.14.14.21 - dibenzothiophene monooxygenase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
homodimer
homohexamer
homotetramer
additional information
homotetramer
enzyme DszC is a tightly associated homotetramer, which can be aptly described as a dimer of dimers
homotetramer
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enzyme DszC is a tightly associated homotetramer, which can be aptly described as a dimer of dimers
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additional information
in the crystal, the homodimeric enzyme forms tetramers from two homodimers, overview
additional information
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in the crystal, the homodimeric enzyme forms tetramers from two homodimers, overview
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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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