Information on EC 1.8.2.4 - dimethyl sulfide:cytochrome c2 reductase

Word Map on EC 1.8.2.4
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 expected taxonomic range for this enzyme is: Rhodovulum sulfidophilum

EC NUMBER
COMMENTARY hide
1.8.2.4
-
RECOMMENDED NAME
GeneOntology No.
dimethyl sulfide:cytochrome c2 reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethyl sulfide + 2 ferricytochrome c2 + H2O = dimethyl sulfoxide + 2 ferrocytochrome c2 + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dimethyl sulfide degradation III (oxidation)
-
-
Sulfur metabolism
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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 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 SUBSTRATES
NATURAL PRODUCTS
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
molybdopterin
[3Fe-4S]-center
subunit DdhB binds one 3Fe-4S cluster
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
-
the enzyme contains 3.5 mol Fe per mol enzyme
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
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
152000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
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; Poros 20HQ Strong anion exchange column chromatography and gel filtration; Poros 20HQ Strong anion exchange column chromatography and gel filtration