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Information on EC 1.8.5.3 - respiratory dimethylsulfoxide reductase and Organism(s) Escherichia coli and UniProt Accession P18775

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IUBMB Comments
The enzyme participates in bacterial electron transfer pathways in which dimethylsulfoxide (DMSO) is the terminal electron acceptor. It is composed of three subunits - DmsA contains a bis(guanylyl molybdopterin) cofactor and a [4Fe-4S] cluster, DmsB is an iron-sulfur protein, and DmsC is a transmembrane protein that anchors the enzyme and accepts electrons from the quinol pool. The electrons are passed through DmsB to DmsA and on to DMSO. The enzyme can also reduce pyridine-N-oxide and trimethylamine N-oxide to the corresponding amines with lower activity.
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UNIPROT: P18775
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
dmso reductase, dimethyl sulfoxide reductase, dmsor, dmsabc, dimethylsulfoxide reductase, dimethyl sulfoxide/trimethylamine n-oxide reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethyl sulfoxide reductase
-
respiratory dimethyl sulfoxide reductase
-
dimethyl sulfoxide reductase
-
-
dimethylsulfoxide reductase
-
-
-
-
DMSO reductase
additional information
-
see also Ec 1.9.6.1
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
dimethyl sulfide:menaquinone oxidoreductase
The enzyme participates in bacterial electron transfer pathways in which dimethylsulfoxide (DMSO) is the terminal electron acceptor. It is composed of three subunits - DmsA contains a bis(guanylyl molybdopterin) cofactor and a [4Fe-4S] cluster, DmsB is an iron-sulfur protein, and DmsC is a transmembrane protein that anchors the enzyme and accepts electrons from the quinol pool. The electrons are passed through DmsB to DmsA and on to DMSO. The enzyme can also reduce pyridine-N-oxide and trimethylamine N-oxide to the corresponding amines with lower activity.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylsulfide + menaquinone + H2O
dimethylsulfoxide + menaquinol
show the reaction diagram
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
show the reaction diagram
-
-
-
?
trimethylamine N-oxide + reduced benzyl viologen
trimethylamine + oxidized benzyl viologen
show the reaction diagram
-
-
-
?
trimethylamine N-oxide + reduced lapachol
trimethylamine + oxidized lapachol
show the reaction diagram
-
-
-
?
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
2-carboxypyridine N-oxide + reduced benzyl viologen + H2O
2-carboxypyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
2-chloropyridine N-oxide + reduced benzyl viologen + H2O
2-chloropyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
2-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
2-hydroxymethylpyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
2-mercaptopyridine N-oxide + reduced benzyl viologen + H2O
2-mercaptopyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
2-methylpyridine N-oxide + reduced benzyl viologen + H2O
2-methylpyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
3-amidopyridine N-oxide + reduced benzyl viologen + H2O
3-amidopyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
3-carboxypyridine N-oxide + reduced benzyl viologen + H2O
3-carboxypyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
3-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
3-hydroxymethylpyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
3-hydroxypyridine N-oxide + reduced benzyl viologen + H2O
3-hydroxypyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
3-methylpyridine N-oxide + reduced benzyl viologen + H2O
3-methylpyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
3alpha-hydroxybenzylpyridine N-oxide + reduced benzyl viologen + H2O
3alpha-hydroxybenzylpyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
4-carboxypyridine N-oxide + reduced benzyl viologen + H2O
4-carboxypyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
4-chloropyridine N-oxide + reduced benzyl viologen + H2O
4-chloropyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
4-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
4-hydroxymethylpyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
4-methylmorpholine N-oxide + reduced benzyl viologen + H2O
4-methylmorpholine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
4-methylpyridine N-oxide + reduced benzyl viologen + H2O
4-methylpyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
4-phenylpyridine N-oxide + reduced benzyl viologen + H2O
4-phenylpyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
dimethyldodecylamine N-oxide + reduced benzyl viologen + H2O
dimethyldodecylamine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
dimethylsulfide + H2O + pyridine N-oxide
dimethylsulfoxide + pyridine
show the reaction diagram
-
-
-
-
?
dimethylsulfoxide + 2,3-dimethyl-1,4-naphthoquinol
dimethylsulfide + H2O + 2,3-dimethyl-1,4-naphthoquinone
show the reaction diagram
-
-
-
-
r
dimethylsulfoxide + methyl viologen
dimethylsulfide + oxidized methyl viologen + H2O
show the reaction diagram
-
activity of mutant C176D of periplasmic nitrate reductase NapA (EC 1.9.6.1), no activity with wild-type NapA or C176S/A NapA mutants
-
-
?
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
r
dimethylsulfoxide + reduced benzyl viologen + H2O
dimethylsulfide + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
dithane 1-oxide + reduced benzyl viologen + H2O
dithane + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
DL-methyl phenyl sulfoxide + reduced benzyl viologen + H2O
DL-methyl phenyl sulfide + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
methionine sulfoxide + reduced benzyl viologen + H2O
methionine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
pyridine N-oxide + reduced benzyl viologen + H2O
pyridine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
tetramethylene sulfoxide + reduced benzyl viologen + H2O
tetramethylene sulfide + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
trimethylamine N-oxide + reduced benzyl viologen + H2O
trimethylamine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
dimethylsulfide + menaquinone + H2O
dimethylsulfoxide + menaquinol
show the reaction diagram
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdenum cofactor
molybdo-bis(pyranopterin guanine dinucleotide)
-
molybdopterin
-
[4Fe-4S]-center
role for the cluster in directing molybdenum cofactor assembly during enzyme maturation. The cluster is predicted to be in close proximity to the molybdo-bis(pyranopterin guanine dinucleotide) cofactor, which provides the site of dimethyl sulfoxide reduction
Fe-S center
methyl viologen
-
-
molybdenum cofactor
-
MoCo, the cofactor coordinates organic molybdopterin to molybdenum, over 50 different molybdopterin enzymes are known to catalyze a variety of chemistries in the cycling of C, N, S, As, and Se, all relying on the same basic cofactor, the MoCo. Kinetic consequences of the exchange of the endogenous ligand to molybdenum with other ligands within the cofactor of DMSO reductase family enzymes, overview. The mutant C176D of periplasmic nitrate reductase NapA (EC 1.9.6.1) is active with DMSO (and artificial cosubstrate methyl viologen), while the wild-type NapA is not
molybdopterin guanine dinucleotide
-
-
additional information
tungsten is present as cofactor in tungsten enzymes, sharing a lot of resemblances with the MoCo of DMSO reductases
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
tungstate
in the presence of the molybdenum antagonist tungstate, wild-type enzyme lacks molybdo-bis(pyranopterin guanine dinucleotide), but is translocated via the Tat translocon and assembles on the periplasmic side of the membrane as an apoenzyme
Molybdenum
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-n-heptyl-4-hydroxyquinoline N-oxide
-
residues Pro80, Ser81, Cys102, and Tyr104 of electron transfer subunit DmsB are located at the DmsB-DmsC interface and are critical for the binding of the MQH2 inhibitor analogue 2-n-heptyl-4-hydroxyquinoline N-oxide
2-n-heptyl-4-hydroxyquinoline-N-oxide
-
menaquinol analogue. 2-n-Heptyl-4-hydroxyquinoline-N-oxide fluorescence is quenched when 2-n-heptyl-4-hydroxyquinoline-N-oxide binds to the holoenzyme DmsABC. The binding stoichiometry is about 1:1. There is one high-affinity 2-n-heptyl-4-hydroxyquinoline-N-oxide binding site per DmsABC molecule located in the DmsC subunit. The interaction follows a two-step equilibrium model, a fast bimolecular step followed by a slow unimolecular step. The quenching of 2-n-heptyl-4-hydroxyquinoline-N-oxide fluorescence occurs in the bimolecular step
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
2-chloropyridine N-oxide
-
pH 7.0, 30°C
0.092
2-methylpyridine N-oxide
-
pH 7.0, 30°C
0.045
3-amidopyridine N-oxide
-
pH 7.0, 30°C
4.94
3-carboxypyridine N-oxide
-
pH 7.0, 30°C
0.094
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
3.17
3-hydroxypyridine N-oxide
-
pH 7.0, 30°C
0.089
3-methylpyridine N-oxide
-
pH 7.0, 30°C
0.158
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30°C
0.513
4-chloropyridine N-oxide
-
pH 7.0, 30°C
0.372
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
11.1
4-methylmorpholine N-oxide
-
pH 7.0, 30°C
0.452
4-methylpyridine N-oxide
-
pH 7.0, 30°C
0.246
4-phenylpyridine N-oxide
-
pH 7.0, 30°C
0.83
dimethyldodecylamine N-oxide
-
pH 7.0, 30°C
0.0282 - 0.18
Dimethylsulfoxide
0.21
DL-methyl phenyl sulfoxide
-
pH 7.0, 30°C
0.09
methionine sulfoxide
-
pH 7.0, 30°C
0.001 - 3.8
Pyridine N-oxide
0.001 - 1.1
reduced benzyl viologen
0.06
tetramethylene sulfoxide
-
pH 7.0, 30°C
20.2
Trimethylamine N-oxide
-
pH 7.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
2-carboxypyridine N-oxide
-
pH 7.0, 30°C
307
2-chloropyridine N-oxide
-
pH 7.0, 30°C
89.3
2-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
8
2-mercaptopyridine N-oxide
-
pH 7.0, 30°C
247
2-methylpyridine N-oxide
-
pH 7.0, 30°C
237
3-amidopyridine N-oxide
-
pH 7.0, 30°C
168
3-carboxypyridine N-oxide
-
pH 7.0, 30°C
214
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
429
3-hydroxypyridine N-oxide
-
pH 7.0, 30°C
231
3-methylpyridine N-oxide
-
pH 7.0, 30°C
229
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30°C
30.3
4-carboxypyridine N-oxide
-
pH 7.0, 30°C
212
4-chloropyridine N-oxide
-
pH 7.0, 30°C
226
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
573
4-methylmorpholine N-oxide
-
pH 7.0, 30°C
268
4-methylpyridine N-oxide
-
pH 7.0, 30°C
297
4-phenylpyridine N-oxide
-
pH 7.0, 30°C
239
dimethyldodecylamine N-oxide
-
pH 7.0, 30°C
0.023 - 79.9
Dimethylsulfoxide
28.4
dithane 1-oxide
-
pH 7.0, 30°C
99.6
DL-methyl phenyl sulfoxide
-
pH 7.0, 30°C
61.1
methionine sulfoxide
-
pH 7.0, 30°C
3 - 940
Pyridine N-oxide
14 - 370
reduced benzyl viologen
119
tetramethylene sulfoxide
-
pH 7.0, 30°C
1203
Trimethylamine N-oxide
-
pH 7.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7130
2-chloropyridine N-oxide
-
pH 7.0, 30°C
2690
2-methylpyridine N-oxide
-
pH 7.0, 30°C
5280
3-amidopyridine N-oxide
-
pH 7.0, 30°C
34
3-carboxypyridine N-oxide
-
pH 7.0, 30°C
2280
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
135
3-hydroxypyridine N-oxide
-
pH 7.0, 30°C
2600
3-methylpyridine N-oxide
-
pH 7.0, 30°C
1450
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30°C
413
4-chloropyridine N-oxide
-
pH 7.0, 30°C
607
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
52
4-methylmorpholine N-oxide
-
pH 7.0, 30°C
592
4-methylpyridine N-oxide
-
pH 7.0, 30°C
1205
4-phenylpyridine N-oxide
-
pH 7.0, 30°C
287
dimethyldodecylamine N-oxide
-
pH 7.0, 30°C
0.816 - 455
Dimethylsulfoxide
483
DL-methyl phenyl sulfoxide
-
pH 7.0, 30°C
663
methionine sulfoxide
-
pH 7.0, 30°C
33 - 10000
Pyridine N-oxide
50 - 23300
reduced benzyl viologen
2080
tetramethylene sulfoxide
-
pH 7.0, 30°C
59
Trimethylamine N-oxide
-
pH 7.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.07
mutant DELTAN21, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
0.14
mutant V20Y/DELTAN21/P27G, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
0.33
mutant V20Y/DELTAN21/P27G/R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
125
mutant R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
141
wild-type, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
2.63
mutant R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
5.22
mutant V20Y/DELTAN21/P27G, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
5.91
mutant DELTAN21, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
7.72
wild-type, cosubstrate lapachol, pH 7.0, temperature not specified in the publication
7.97
mutant V20Y/DELTAN21/P27G/R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
recombinant NapA mutant C176D
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
activity range, recombinant NapA mutant C176D
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
overexpression of membrane anchor subunit DmsC tagged with a dystrophin-specific amino acid sequence in COS-1 or Mc-RH777 cells, results in localization to endoplasmic reticulum
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
evolution
-
respiratory enzyme members of the DMSOR family such as nitrate reductase (NR, EC 1.9.6.1), dimethyl sulfoxide reductase (DMSOR, EC 1.8.5.3), trimethylamine N-oxide reductase (TMAOR, EC 1.7.2.3), and formate dehydrogenase (FDH) contribute to this broad diversity. The DMSOR family of enzymes has diverse active sites that vary in the first coordination sphere of the molybdenum center. Many enzymes in the DMSOR family use oxygen atom transfer (OAT) reactions for substrate transformation, e.g. periplasmic nitrate reductase (Nap) and respiratory nitrate reductase (Nar) reduce nitrate to nitrite, TMAOR reduces TMAO to TMA, and DMSOR reduces DMSO to dimethyl sulfide (DMS). Enzymes that catalyze the same reaction, such as Nap and Nar, have different molybdenum coordination spheres. In NapA, molybdenum is coordinated by a cysteine residue in the 5th position and an oxo or a sulfido group in the 6th
physiological function
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the DmsAB dimer is thermolabile and catalyzes the reduction of various substrates in the presence of artificial electron donors. Results suggest that the membrane-intrinsic subunit DmsC is necessary for anchoring, stability, and electron transport. The C-terminal region of DmsB appears to interact with the anchor peptide and facilitates the membrane assembly of the catalytic dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray absorption spectroscopic analysis of the molybdenum active site of Escherichia coli dimethyl sulfoxide reductase contained within its native membranes.The oxidized active site has four Mo-S ligands at 2.43 A, one Mo=O at 1.71 A, and a longer Mo-O at 1.90 A. The oxidized enzyme is a monooxomolybdenum(VI) species coordinated by two molybdopterin dithiolenes and a serine. Results suggest that the form found in vivo is the monooxobis(molybdopterin) species
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C59S
mutantion renders enzyme maturation sensitive to molybdenum cofactor availability. Residue C59 is a ligand to the FS0 [4Fe-4S] cluster. In the presence of trace amounts of molybdate, the C59S variant assembles normally to the cytoplasmic membrane and supports respiratory growth on DMSO, although the ground state of FS0 as determined by EPR is converted from high-spin, S = 3/2, to low-spin, S = 1/2. In the presence of the molybdenum antagonist tungstate, wild-type enzyme lacks molybdo-bis(pyranopterin guanine dinucleotide), but is translocated via the Tat translocon and assembles on the periplasmic side of the membrane as an apoenzyme. The C59S variant cannot overcome the dual insults of amino acid substitution plus lack of molybdo-bis(pyranopterin guanine dinucleotide) , leading to degradation of the DmsABC subunits
DELTAN21
mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled
R61K
molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity
V20Y/DELTAN21/P27G
introduction of a type I Cys group, mutations eliminate both molybdo-bis(pyranopterin guanine dinucleotide) binding and detection of a FSo cluster by EPR
V20Y/DELTAN21/P27G/R61K
addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion
A178Q
A181T
-
mutation in subunit DmsA. About 300% of wild-type catalytic efficiency
C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. The midpoint potential of FS4[3Fe-4S] is insensitive to inhibitor 2-n-heptyl-4-hydroxyquinoline N-oxide as well as to changes in pH from 5 to 7
C38S
-
the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is significantly modified in DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA. In ferricyanide-oxidized glycerol-inhibited DmsAC38SBC, there is no detectable interaction between the oxidized [3Fe-4S] cluster and the molybdo bis(molybdopterin guanine dinucleotide) cofactor
D95A
-
mutation in electron transfer subunit DmsB
D95A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D95K/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D97A
-
mutation in electron transfer subunit DmsB
D97A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
G167N
G190D
-
mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
G190V
-
mutation in subunit DmsA. About 180% of wild-type catalytic efficiency
H106A
-
mutation in electron transfer subunit DmsB
H106A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106E
-
mutation in electron transfer subunit DmsB
H106E/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106I/C102S 2
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H65R
-
mutation in subunit DmsC. Mutant blocks binding of the menaquinol analogue 2-n-heptyl-4-hydroxyquinoline-N-oxide to the protein
H85F
-
mutation in electron transfer subunit DmsB
H85F/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H85T
-
mutation in electron transfer subunit DmsB
H85T/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
K77A
-
mutation in electron transfer subunit DmsB
K77A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
M147I
-
mutation in subunit DmsA. About 65% of wild-type catalytic efficiency
M147L
-
mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
P80A
-
mutation in electron transfer subunit DmsB
P80A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
P80D
-
mutation in electron transfer subunit DmsB
P80H
-
mutation in electron transfer subunit DmsB
Q179I
R103A
-
mutation in electron transfer subunit DmsB
R103A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
R149C
-
mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
R217Q
R77S
-
DmsA-R77S mutant, the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is eliminated
S176A/C102S
-
double mutant DmsA-S176A and DmsB-C102S, contains an engineered [3Fe-4S] cluster in DmsB, no significant paramagnetic interaction is detected between the oxidized [3Fe-4S] cluster and the Mo(V)
S81G
-
mutation in electron transfer subunit DmsB
S81H
-
mutation in electron transfer subunit DmsB
T148S
W191G
-
mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
W357C
-
mutation in subunit DmsA. About 100% of wild-type catalytic efficiency
W357F
-
mutation in subunit DmsA. About 40% of wild-type catalytic efficiency
W357Y
-
mutation in subunit DmsA. About 60% of wild-type catalytic efficiency
Y104A
-
mutation in electron transfer subunit DmsB
Y104A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104D
-
mutation in electron transfer subunit DmsB
Y104D/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 150 mV. The midpoint potential of FS4 increases in the presence of 2-n-heptyl-4-hydroxyquinoline N-oxide and decreasing pH
Y104D/H106F/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104E 
-
mutation in electron transfer subunit DmsB
Y104E/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 145 mV
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
15 min, inactivation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dmsA, DNA and amino acid sequence comparisons and phylogenetic analysis, detailed overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, V.W.; Rothery, R.A.; Bertero, M.G.; Strynadka, N.C.; Weiner, J.H.
Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase
Biochemistry
44
8068-8077
2005
Escherichia coli
Manually annotated by BRENDA team
Miguel, L.; Meganthan, R.
Electron donors and the quinone involved in dimethyl sulfoxide reduction in Escherichia coli
Curr. Microbiol.
22
109-115
1991
Escherichia coli
-
Manually annotated by BRENDA team
Simala-Grant, J.L.; Weiner, J.H.
Modulation of the substrate specificity of Escherichia coli dimethylsulfoxide reductase
Eur. J. Biochem.
251
510-515
1998
Escherichia coli
Manually annotated by BRENDA team
Daruwala, R.; Meganathan, R.
Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli
FEMS Microbiol. Lett.
83
255-259
1991
Escherichia coli
Manually annotated by BRENDA team
George, G.; Doonan, C.; Rothery, R.; Boroumand, N.; Weiner, J.
X-ray absorption spectroscopic characterization of the molybdenum site of Escherichia coli dimethyl sulfoxide reductase
Inorg. Chem.
46
2-4
2007
Escherichia coli
Manually annotated by BRENDA team
Sambasivarao, D.; Weiner, J.
Dimethyl sulfoxide reductase of Escherichia coli: An investigation of function and assembly by use of in vivo complementation
J. Bacteriol.
173
5935-5943
1991
Escherichia coli
Manually annotated by BRENDA team
Zhao, Z.; Weiner, J.
Interaction of 2-n-heptyl-4-hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli
J. Biol. Chem.
273
20758-20763
1998
Escherichia coli
Manually annotated by BRENDA team
Rothery, R.A.; Trieber, C.A.; Weiner, J.H.
Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase
J. Biol. Chem.
274
13002-13009
1999
Escherichia coli
Manually annotated by BRENDA team
Simala-Grant, J.; Weiner, J.
Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase
Microbiology
142
3231-3239
1996
Escherichia coli
Manually annotated by BRENDA team
Hanlon, S.; Graham, D.; Hogan, P.; Holt, R.; Reeve, C.; Shaw, A.; McEwan, A.
Asymmetric reduction of racemic sulfoxides by dimethyl sulfoxide reductases from Rhodobacter capsulatus, Escherichia coli and Proteus species
Microbiology
144
2247-2253
1998
Escherichia coli, Proteus mirabilis, Rhodobacter capsulatus
Manually annotated by BRENDA team
Turner, R.; Busaan, J.; Lee, J.; Michalak, M.; Weiner, J.
Expression and epitope tagging of the membrane anchor subunit (DmsC) of Escherichia coli dimethyl sulfoxide reductase
Protein Eng.
10
285-290
1997
Escherichia coli
Manually annotated by BRENDA team
Tang, H.; Rothery, R.A.; Weiner, J.H.
A variant conferring cofactor-dependent assembly of Escherichia coli dimethylsulfoxide reductase
Biochim. Biophys. Acta
1827
730-737
2013
Escherichia coli (P18775), Escherichia coli
Manually annotated by BRENDA team
Tang, H.; Rothery, R.A.; Voss, J.E.; Weiner, J.H.
Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion
J. Biol. Chem.
286
15147-15154
2011
Escherichia coli (P18775), Escherichia coli
Manually annotated by BRENDA team
Ha, Y.; Tenderholt, A.L.; Holm, R.H.; Hedman, B.; Hodgson, K.O.; Solomon, E.I.
Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on monooxo Mo(IV) and bisoxo Mo(VI) bis-dithiolenes insights into the mechanism of oxo transfer in sulfite oxidase and its relation to the mechanism of DMSO reductase
J. Am. Chem. Soc.
136
9094-9105
2014
Escherichia coli (P18775)
Manually annotated by BRENDA team
Miralles-Robledillo, J.M.; Torregrosa-Crespo, J.; Martinez-Espinosa, R.M.; Pire, C.
DMSO reductase family phylogenetics and applications of extremophiles
Int. J. Mol. Sci.
20
3349
2019
Escherichia coli (P18775), Halobacterium salinarum (Q9HR74), Escherichia coli K12 (P18775), Halobacterium salinarum ATCC 700922 (Q9HR74), Halobacterium salinarum JCM 11081 (Q9HR74)
Manually annotated by BRENDA team
Mintmier, B.; McGarry, J.M.; Bain, D.J.; Basu, P.
Kinetic consequences of the endogenous ligand to molybdenum in the DMSO reductase family a case study with periplasmic nitrate reductase
J. Biol. Inorg. Chem.
26
13-28
2021
Escherichia coli
Manually annotated by BRENDA team
Wells, M.; Kanmanii, N.J.; Al Zadjali, A.M.; Janecka, J.E.; Basu, P.; Oremland, R.S.; Stolz, J.F.
Methane, arsenic, selenium and the origins of the DMSO reductase family
Sci. Rep.
10
10946
2020
Escherichia coli (P18775)
Manually annotated by BRENDA team