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Information on EC 1.8.2.4 - dimethyl sulfide:cytochrome c2 reductase
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1.8.2.4 dimethyl sulfide:cytochrome c2 reductaseIUBMB Comments
The enzyme from the bacterium Rhodovulum sulfidophilum binds molybdopterin guanine dinucleotide, heme b and [4Fe-4S] clusters.
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Word Map
- 1.8.2.4
-
rhodovulum
- sulfidophilum
- dmso
- molybdenum
- sulfoxide
- selenate
- heme
- ethylbenzene
-
heterotrimeric
- nitrate
- guanine
- beta-subunits
-
bismolybdopterin
- epr
- alpha-subunits
- narghi
-
photolithotrophic
-
photochemical
- fe-s
-
b-type
-
potentiometry
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
DdhA, DdhB, DdhC, dimethyl sulfide dehydrogenase, dimethyl sulphide dehydrogenase, dimethylsulfide: acceptor oxidoreductase, DMS dehydrogenase, DMS DH, DMS:ferricytochrome c2 oxidoreductase, Me2S:acceptor oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DdhA
DdhB
DdhC
dimethyl sulfide dehydrogenase
dimethyl sulphide dehydrogenase
DMS dehydrogenase
DMS DH
DMS:ferricytochrome c2 oxidoreductase
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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PATHWAY SOURCE
PATHWAYS
KEGG
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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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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
-
-
-
-
?
dimethyl sulfoxide + reduced methyl viologen + H2O
dimethyl sulfide + oxidized methyl viologen
-
2% activity compared to trimethylamine N-oxide
-
-
?
lauryldimethylamine N-oxide + reduced methyl viologen + H2O
?
-
69% activity compared to trimethylamine N-oxide
-
-
?
trimethylamine N-oxide + reduced methyl viologen + H2O
?
-
100% activity
-
-
?
additional information
?
-
-
no activity with chlorate and bromate
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
?
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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NATURAL SUBSTRATE
NATURAL 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 + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
-
-
-
?
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
the enzyme contains 17 mol iron per mol enzyme
Molybdenum
Molybdenum
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
-
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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
-
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A379SJU5_SALER
1020
0
110903
TrEMBL
-
A0A447JHC8_SALET
1020
0
110985
TrEMBL
-
A0A1J5RYR3_9ZZZZ
914
0
100551
TrEMBL
other Location (Reliability: 2)
A0A3B1CUR7_9ZZZZ
772
0
86572
TrEMBL
other Location (Reliability: 4)
A0A379SVH9_SALER
1020
0
110919
TrEMBL
-
A0A447NV59_SALET
722
0
78747
TrEMBL
-
A0A143X6Z2_9ACTN
909
0
101893
TrEMBL
-
A0A6D2G8D7_SALER
421
0
46087
TrEMBL
-
A0A3B1BV75_9ZZZZ
940
1
105288
TrEMBL
other Location (Reliability: 5)
A0A259U9M8_9FIRM
894
0
100145
TrEMBL
-
A0A0T7RNC4_SALET
1020
0
110981
TrEMBL
-
A0A2X4TCN4_SALER
1020
0
110889
TrEMBL
-
A0A379XQS6_SALER
1020
0
111045
TrEMBL
-
A0A1V4AZ11_9PAST
1029
0
113620
TrEMBL
-
A0A143X7Q0_9ACTN
941
0
104305
TrEMBL
-
A0A379TBJ7_SALER
168
0
18482
TrEMBL
-
A0A143X7X2_9ACTN
815
0
89497
TrEMBL
-
S0G7M7_9DELT
814
0
91966
TrEMBL
-
A0A379S560_SALER
521
0
56678
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
38000
94000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
heterotrimer
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
-
ammonium sulfate precipitation, SP-Sepharose column chromatography, gel filtration
-
Poros 20HQ Strong anion exchange column chromatography and gel filtration
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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
brenda
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
brenda
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)
brenda
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