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Information on EC 1.8.2.4 - dimethyl sulfide:cytochrome c2 reductase and Organism(s) Rhodovulum sulfidophilum and UniProt Accession Q8GPG4

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IUBMB Comments
The enzyme from the bacterium Rhodovulum sulfidophilum binds molybdopterin guanine dinucleotide, heme b and [4Fe-4S] clusters.
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This record set is specific for:
Rhodovulum sulfidophilum
UNIPROT: Q8GPG4
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The taxonomic range for the selected organisms is: Rhodovulum sulfidophilum
The enzyme appears in selected viruses and cellular organisms
Synonyms
dms dehydrogenase, dimethyl sulfide dehydrogenase, dimethyl sulphide dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethyl sulphide dehydrogenase
-
DMS dehydrogenase
-
dimethyl sulfide dehydrogenase
-
-
dimethyl sulphide dehydrogenase
-
dimethylsulfide: acceptor oxidoreductase
-
-
DMS dehydrogenase
DMS:ferricytochrome c2 oxidoreductase
-
-
Me2S:acceptor oxidoreductase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
show the reaction diagram
-
-
-
?
dimethyl sulfide + oxidized 2,6-dichlorophenolindophenol + H2O
dimethyl sulfoxide + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
show the reaction diagram
dimethyl sulfide + oxidized 2,6-dichlorophenolindophenol + H2O
dimethyl sulfoxide + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
dimethyl sulfoxide + reduced 2,6-dichloroindophenol
dimethyl sulfide + oxidized 2,6-dichloroindophenol + H2O
show the reaction diagram
-
-
-
-
?
dimethyl sulfoxide + reduced methyl viologen + H2O
dimethyl sulfide + oxidized methyl viologen
show the reaction diagram
-
2% activity compared to trimethylamine N-oxide
-
-
?
lauryldimethylamine N-oxide + reduced methyl viologen + H2O
?
show the reaction diagram
-
69% activity compared to trimethylamine N-oxide
-
-
?
trimethylamine N-oxide + reduced methyl viologen + H2O
?
show the reaction diagram
-
100% activity
-
-
?
additional information
?
-
-
no activity with chlorate and bromate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
show the reaction diagram
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdopterin
bis(molybdopterin guanine dinucleotide)Mo
iron-sulfur centre
molybdopterin
[3Fe-4S]-center
subunit DdhB binds one 3Fe-4S cluster
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the enzyme contains 17 mol iron per mol enzyme
Molybdenum
the enzyme contains 0.5 mol molybdenum per mol enzyme
Fe
-
the enzyme contains 3.5 mol Fe per mol enzyme
Iron
the enzyme contains 17 mol iron per mol enzyme
Molybdenum
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.053
Dimethyl sulfide
-
in 220 mM Tris-HCl pH 8.0, 22°C
0.021
ferricytochrome c2
-
in 220 mM Tris-HCl pH 8.0, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18.2
-
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
-
after purification, using reduced 2,6-dichloroindophenol as cosubstrate, in 50 mM Tris/HCI pH 8.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit alpha (DdhA)
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the ddhA mutant is not able to grow photoautotrophically with dimethyl sulfide as electron donor, although photoheterotrophic growth is not impaired
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DDHA_RHOSU
910
0
102309
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
1 * 94000 + 1 * 38000 + 1 * 32000
38000
1 * 94000 + 1 * 38000 + 1 * 32000
152000
-
gel filtration
32000
38000
94000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
1 * 94000 + 1 * 38000 + 1 * 32000
heterotrimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Poros 20HQ Strong anion exchange column chromatography and gel filtration
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, hydroxyapatite column chromatography, and Sephacryl S-200 gel filtration
-
ammonium sulfate precipitation, SP-Sepharose column chromatography, gel filtration
-
Poros 20HQ Strong anion exchange column chromatography and gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hanlon, S.; Toh, T.; Solomon, P.; Holt, R.; McEwan, A.
Dimethylsulfide: acceptor oxidoreductase from Rhodobacter sulfidophilus - The purified enzyme contains b-type haem and a pterin molybdenum cofactor
Eur. J. Biochem.
239
391-396
1996
Rhodovulum sulfidophilum
Manually annotated by BRENDA team
Creevey, N.; McEwan, A.; Bernhardt, P.
A mechanistic and electrochemical study of the interaction between dimethyl sulfide dehydrogenase and its electron transfer partner cytochrome c2
J. Biol. Inorg. Chem.
13
1231-1238
2008
Rhodovulum sulfidophilum, Rhodovulum sulfidophilum SH1
Manually annotated by BRENDA team
McDevitt, C.; Hugenholtz, P.; Hanson, G.; McEwan, A.
Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: Its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes
Mol. Microbiol.
44
1575-1587
2002
Rhodovulum sulfidophilum (Q8GPG1), Rhodovulum sulfidophilum (Q8GPG3), Rhodovulum sulfidophilum (Q8GPG4), Rhodovulum sulfidophilum, Rhodovulum sulfidophilum SH1 (Q8GPG1), Rhodovulum sulfidophilum SH1 (Q8GPG3), Rhodovulum sulfidophilum SH1 (Q8GPG4)
Manually annotated by BRENDA team