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Enzyme Nomenclature
Information on EC 1.8.2.4 - dimethyl sulfide:cytochrome c2 reductase
for references in articles please use BRENDA:EC1.8.2.4
Word Map on EC 1.8.2.4
- 1.8.2.4
- dmso
-
rhodovulum
- sulfidophilum
- molybdenum
- sulfoxide
- heme
- ethylbenzene
-
heterotrimeric
- nitrate
- selenate
-
bismolybdopterin
-
beta-subunits
- epr
-
b-type
-
potentiometry
-
photolithotrophic
- narghi
-
alpha-subunits
- guanine
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photochemical
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The expected taxonomic range for this enzyme is: Rhodovulum sulfidophilum
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EC NUMBER 
COMMENTARY 
1.8.2.4
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RECOMMENDED NAME
GeneOntology No.
dimethyl sulfide:cytochrome c2 reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethyl sulfide + 2 ferricytochrome c2 + H2O = dimethyl sulfoxide + 2 ferrocytochrome c2 + 2 H+
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
dimethyl sulfide:ferricytochrome-c2 oxidoreductase
The enzyme from the bacterium Rhodovulum sulfidophilum binds molybdopterin guanine dinucleotide, heme b and [4Fe-4S] clusters.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
the ddhA mutant is not able to grow photoautotrophically with dimethyl sulfide as electron donor, although photoheterotrophic growth is not impaired
malfunction
-
the ddhA mutant is not able to grow photoautotrophically with dimethyl sulfide as electron donor, although photoheterotrophic growth is not impaired
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physiological function
dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate; dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate; dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate
physiological function
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dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate; dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate; dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate
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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
dimethyl sulfide + oxidized 2,6-dichlorophenolindophenol + H2O
dimethyl sulfoxide + reduced 2,6-dichlorophenolindophenol
dimethyl sulfoxide + reduced 2,6-dichloroindophenol
dimethyl sulfide + oxidized 2,6-dichloroindophenol + H2O
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-
-
-
?
dimethyl sulfoxide + reduced methyl viologen + H2O
dimethyl sulfide + oxidized methyl viologen
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2% activity compared to trimethylamine N-oxide
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-
?
lauryldimethylamine N-oxide + reduced methyl viologen + H2O
?
-
69% activity compared to trimethylamine N-oxide
-
-
?
trimethylamine N-oxide + reduced methyl viologen + H2O
?
-
100% activity
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-
?
additional information
?
-
-
no activity with chlorate and bromate
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-
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dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism
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-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism
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-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
?
dimethyl sulfide + oxidized 2,6-dichlorophenolindophenol + H2O
dimethyl sulfoxide + reduced 2,6-dichlorophenolindophenol
-
-
-
?
dimethyl sulfide + oxidized 2,6-dichlorophenolindophenol + H2O
dimethyl sulfoxide + reduced 2,6-dichlorophenolindophenol
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-
-
?
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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
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
Q8GPG1, Q8GPG3, Q8GPG4
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-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
Q8GPG1, Q8GPG3, Q8GPG4
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[3Fe-4S]-center
subunit DdhB binds one 3Fe-4S cluster
heme
-
the cytochrome contains a b-type heme and a content of 0.65 mol protoheme per mol enzyme is determined
molybdopterin
bis(molybdopterin guanine dinucleotide)Mo; bis(molybdopterin guanine dinucleotide)Mo; bis(molybdopterin guanine dinucleotide)Mo
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
the enzyme contains 17 mol iron per mol enzyme; the enzyme contains 17 mol iron per mol enzyme; the enzyme contains 17 mol iron per mol enzyme
Molybdenum
Molybdenum
the enzyme contains 0.5 mol molybdenum per mol enzyme; the enzyme contains 0.5 mol molybdenum per mol enzyme; the enzyme contains 0.5 mol molybdenum per mol enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18.2
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crude extract, using reduced 2,6-dichloroindophenol as cosubstrate, in 50 mM Tris/HCI pH 8.0, temperature not specified in the publication
20.2
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after purification, using reduced 2,6-dichloroindophenol as cosubstrate, in 50 mM Tris/HCI pH 8.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
38000
94000
32000
1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; subunit DdhC
38000
1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; subunit DdhB
94000
1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; subunit DdhA
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
heterotrimer
1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000
heterotrimer
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; 1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, hydroxyapatite column chromatography, and Sephacryl S-200 gel filtration
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ammonium sulfate precipitation, SP-Sepharose column chromatography, gel filtration
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Poros 20HQ Strong anion exchange column chromatography and gel filtration; Poros 20HQ Strong anion exchange column chromatography and gel filtration; Poros 20HQ Strong anion exchange column chromatography and gel filtration
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.2.4)
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