Information on EC 1.14.14.22 - dibenzothiophene sulfone monooxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.22
-
RECOMMENDED NAME
GeneOntology No.
dibenzothiophene sulfone monooxygenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2 = 2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dibenzothiophene desulfurization
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene bdsA
-
-
Manually annotated by BRENDA team
gene bdsA
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Gordonia sp. F.5.25.8
-
-
-
Manually annotated by BRENDA team
gene tdsA
UniProt
Manually annotated by BRENDA team
gene tdsA
UniProt
Manually annotated by BRENDA team
gene dszA
UniProt
Manually annotated by BRENDA team
isolate SA21, gene dszA
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
show the reaction diagram
2-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
show the reaction diagram
3,4,6-trimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
show the reaction diagram
3,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
show the reaction diagram
3-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
show the reaction diagram
-
-
-
-
?
3-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
? + 2 FMN + H2O
show the reaction diagram
4,6-dimethyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
show the reaction diagram
-
-
-
-
?
4-methyldibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
?
show the reaction diagram
-
-
-
-
?
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
show the reaction diagram
dibenz[c,e][1,2] oxathiin 6-oxide + 2 FMNH2 + O2
2,2'-dihydroxybiphenyl + 2 FMN + H2O
show the reaction diagram
dibenz[c,e][1,2]oxathiin 6,6-dioxide + 2 FMNH2 + O2
2,2'-dihydroxybiphenyl + 2 FMN + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dibenzothiophene-5,5-dioxide + 2 FMNH2 + O2
2'-hydroxybiphenyl-2-sulfinate + 2 FMN + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMNH2
NADH
-
the enzyme does not directly react with NADH, but uses the activity of the FMN:NADH oxidoreductase, DszD
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5,5'-dithiobis(2-nitrobenzoic acid)
-
slightly activating at 0.1 mM
Cd2+
-
slightly activating at 1 mM
Mg2+
-
slight activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-biphenyl
-
-
-
2,2'-bipyridine
-
-
2,2-bipyridine
-
62% inhibition at 1 mM
4-chloromercuribenzoate
-
-
4-chloromercuribenzoic acid
-
-
5,5'-dithio-bis-2-nitrobenzoic acid
-
-
8-Quinolinol
-
; 88% inhibition at 1 mM
Fe2+
-
32% inhibition at 1 mM
iodoacetic acid
-
-
Li+
-
20% inhibition at 1 mM
N-bromosuccinimide
-
17% inhibition at 1 mM
N-ethylmaleimide
NO3-
-
39% inhibition at 1 mM
p-chloromercuribenzoic acid
-
50% inhibition at 1 mM
sulfate
-
slightly inhibiting
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
807
-
purified enzyme, pH 7.0, 35°C
855
-
purified native enzyme, pH 7.0, 50°C
875
-
purified recombinant enzyme, pH 7.0, 50°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 35
-
assay at
37 - 50
-
assay at, cell extract
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 65
-
activity range, profile overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38900
-
x * 38900, about, sequnence calculation
45000
-
4 * 45000, SDS-PAGE
48000
-
2 * 48000, SDS-PAGE
49579
-
2 * 49579, sequence calculation
50000
-
2 * 50000, SDS-PAGE
97000
-
gel filtration
100000
-
gel filtration
120000
-
gel filtration
174000
-
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
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
-
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
purified enzyme, stable up to
50
-
purified enzyme, 30 min, 30% activity remaning
60
-
purified enzyme, pH 7.0, highly stable up to
70
-
purified enzyme, pH 7.0, inactivation
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
-
native enzyme to homogeneity by anion exchange and hydrophobic interaction chromatography, and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain DH5alpha by nickel affinty chromatography
-
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
-
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
-
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
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information