Information on EC 1.8.5.3 - dimethylsulfoxide reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.8.5.3
-
RECOMMENDED NAME
GeneOntology No.
dimethylsulfoxide reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
formate to dimethyl sulfoxide electron transfer
-
-
hydrogen to dimethyl sulfoxide electron transfer
-
-
NADH to dimethyl sulfoxide electron transfer
-
-
Sulfur metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
dimethyl sulfide:menaquinone oxidoreductase
Contains molybdopterin and [4Fe-4S] clusters. Also reduces pyridine N-oxide and trimethylamine N-oxide, with lower activity, to the corresponding amines.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
(ethylsulfinyl)benzene + reduced benzyl viologen
(ethylsulfanyl)benzene + H2O + oxidized benzyl viologen
show the reaction diagram
(methylsulfinyl)benzene + reduced benzyl viologen
(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
show the reaction diagram
(propan-2-ylsulfinyl)benzene + reduced benzyl viologen
(propan-2-ylsulfanyl)benzene + H2O + oxidized benzyl viologen
show the reaction diagram
(propylsulfanyl)benzene + reduced benzyl viologen
(propylsulfinyl)benzene + H2O + oxidized benzyl viologen
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
(S)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
(S)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
(S)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
show the reaction diagram
-
catalyses the selective removal of (S)-methyl p-tolyl sulfoxide from a racemic mixture of methyl p-tolyl sulfoxide, resulting in an 88 O/o recovery of enantiomerically pure (R)-methyl p-tolyl sulfoxide
-
-
?
(S)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
1-bromo-4-(methylsulfinyl)benzene + reduced benzyl viologen
1-bromo-4-(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
show the reaction diagram
-
180% of the rate with dimethysulfoxide
-
-
?
1-methyl-4-(methylsulfinyl)benzene + reduced benzyl viologen
1-methyl-4-(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
show the reaction diagram
-
150% of the rate with dimethysulfoxide
-
-
?
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
-
-
-
-
?
adenosine-1N-oxide + reduced dichlorophenolindophenol
adenine + H2O + oxidized dichlorophenolindophenol
show the reaction diagram
-
-
-
-
r
dimethyl sulfoxide + reduced methyl viologen
dimethyl sulfide + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
r
dimethyldodecylamine N-oxide + reduced benzyl viologen + H2O
dimethyldodecylamine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
dimethylsulfide + H2O + oxidized benzyl viologen
dimethylsulfoxide + reduced benzyl viologen
show the reaction diagram
-
-
-
-
r
dimethylsulfide + H2O + oxidized methyl viologen
dimethylsulfoxide + reduced methyl viologen
show the reaction diagram
-
-
-
-
r
dimethylsulfide + H2O + pyridine N-oxide
dimethylsulfoxide + pyridine
show the reaction diagram
-
-
-
-
?
dimethylsulfoxide + 2,3-dimethyl-1,4-napthoquinol
dimethylsulfide + H2O + 2,3-dimethyl-1,4-napthoquinone
show the reaction diagram
-
-
-
-
r
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
show the reaction diagram
dimethylsulfoxide + reduced benzyl viologen + H2O
dimethylsulfide + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
dimethylsulfoxide + reduced dichlorophenolindophenol
dimethylsulfide + H2O + oxidized dichlorophenolindophenol
show the reaction diagram
-
-
-
-
r
dimethylsulfoxide + reduced methyl viologen
dimethylsulfide + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
r
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
-
-
-
-
?
methionine sulfoxide + reduced dichlorophenolindophenol
methionine + H2O + oxidized dichlorophenolindophenol
show the reaction diagram
-
-
-
-
r
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
trimethylamine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
trimethylamine N-oxide + reduced benzyl viologen + H2O
trimethylamine + oxidized benzyl viologen
show the reaction diagram
-
-
-
-
?
trimethylamine N-oxide + reduced dichlorophenolindophenol
trimethylamine + H2O + oxidized dichlorophenolindophenol
show the reaction diagram
-
-
-
-
r
trimethylamine N-oxide + reduced lapachol
trimethylamine + oxidized lapachol
show the reaction diagram
-
-
-
-
?
trimethylamine-N-oxide + reduced methyl viologen
trimethylamine + H2O + oxidized methyl viologen
show the reaction diagram
-
-
-
-
r
[(methylsulfinyl)methyl]benzene + reduced benzyl viologen
[(methylsulfanyl)methyl]benzene + H2O + oxidized benzyl viologen
show the reaction diagram
-
130% of the rate with dimethysulfoxide
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
Fe-S center
molybdenum bis-molybdopterin guanine dinucleotide
molybdenum cofactor
-
residue W116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affects the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm. W116 plays a critical role in stabilizing the hexacoordinate monooxo MoVI form of the enzyme and prevents the formation of a dioxo pentacoordinate MoVI species
molybdo-bis(pyranopterin guanine dinucleotide)
-
-
molybdopterin guanine dinucleotide
-
-
[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
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
Tungsten
INHIBITORS
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, 30C
0.092
2-methylpyridine N-oxide
-
pH 7.0, 30C
0.045
3-amidopyridine N-oxide
-
pH 7.0, 30C
4.94
3-carboxypyridine N-oxide
-
pH 7.0, 30C
0.094
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30C
3.17
3-hydroxypyridine N-oxide
-
pH 7.0, 30C
0.089
3-methylpyridine N-oxide
-
pH 7.0, 30C
0.158
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30C
0.513
4-chloropyridine N-oxide
-
pH 7.0, 30C
0.372
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30C
11.1
4-methylmorpholine N-oxide
-
pH 7.0, 30C
0.452
4-methylpyridine N-oxide
-
pH 7.0, 30C
0.246
4-phenylpyridine N-oxide
-
pH 7.0, 30C
0.02 - 0.52
adenosine-1N-oxide
0.83
dimethyldodecylamine N-oxide
-
pH 7.0, 30C
0.007 - 0.4
Dimethylsulfoxide
0.21
DL-methyl phenyl sulfoxide
-
pH 7.0, 30C
0.09 - 19
methionine sulfoxide
0.001 - 3.8
Pyridine N-oxide
0.001 - 1.1
reduced benzyl viologen
0.06
tetramethylene sulfoxide
-
pH 7.0, 30C
2.3 - 88
Trimethylamine N-oxide
0.0959 - 0.193
Trimethylamine-N-oxide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8
2-carboxypyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
307
2-chloropyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
89.3
2-hydroxymethylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
8
2-mercaptopyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
247
2-methylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
237
3-amidopyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
168
3-carboxypyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
214
3-hydroxymethylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
429
3-hydroxypyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
231
3-methylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
229
3alpha-hydroxybenzylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
30.3
4-carboxypyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
212
4-chloropyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
226
4-hydroxymethylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
573
4-methylmorpholine N-oxide
Escherichia coli
-
pH 7.0, 30C
268
4-methylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
297
4-phenylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
110 - 2200
adenosine-1N-oxide
21 - 470
dimethyl sulfoxide
239
dimethyldodecylamine N-oxide
Escherichia coli
-
pH 7.0, 30C
8
Dimethylsulfide
Rhodobacter capsulatus
-
pH 8.0, 25C
7 - 180
Dimethylsulfoxide
28.4
dithane 1-oxide
Escherichia coli
-
pH 7.0, 30C
99.6
DL-methyl phenyl sulfoxide
Escherichia coli
-
pH 7.0, 30C
58 - 180
methionine sulfoxide
3 - 940
Pyridine N-oxide
14 - 370
reduced benzyl viologen
27
reduced methyl viologen
Rhodobacter capsulatus
-
pH 8.0, 25C
119
tetramethylene sulfoxide
Escherichia coli
-
pH 7.0, 30C
1203 - 4300
Trimethylamine N-oxide
11.3 - 134.5
Trimethylamine-N-oxide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7130
2-chloropyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
11171
2690
2-methylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
41309
5280
3-amidopyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
41308
34
3-carboxypyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
41316
2280
3-hydroxymethylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
41310
135
3-hydroxypyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
13257
2600
3-methylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
28110
1450
3alpha-hydroxybenzylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
41311
413
4-chloropyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
11179
607
4-hydroxymethylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
41313
52
4-methylmorpholine N-oxide
Escherichia coli
-
pH 7.0, 30C
5722
592
4-methylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
41314
1205
4-phenylpyridine N-oxide
Escherichia coli
-
pH 7.0, 30C
41312
4200 - 15000
adenosine-1N-oxide
12146
287
dimethyldodecylamine N-oxide
Escherichia coli
-
pH 7.0, 30C
41315
170 - 7100
Dimethylsulfoxide
985
483
DL-methyl phenyl sulfoxide
Escherichia coli
-
pH 7.0, 30C
41317
5.8 - 663
methionine sulfoxide
4830
33 - 10000
Pyridine N-oxide
1688
50 - 23300
reduced benzyl viologen
325
2080
tetramethylene sulfoxide
Escherichia coli
-
pH 7.0, 30C
9607
34 - 830
Trimethylamine N-oxide
1480
100 - 700
Trimethylamine-N-oxide
5623
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
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
reduction of dimethyl sulfoxide
8.3
-
oxidation of dimethyl sulfide
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
-
x * 90000, calculated
SUBUNITS
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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
-
damaged enzyme form derived from an intermediate formed by reaction of DMSOR with dimethylsulfide and reaction with oxygen, to 2.0 A resolution. All four thiolate ligands and Ogamma of serine-147 remain coordinated to molybdenum, there are no terminal oxygen ligands and molybdenum is Mo(VI)
-
protein with tungsten in place of molybdenum, to 2.0 A resolution
-
to 1.88 A resolution, space group P41212. Spherical protein, consists of four domains with a funnel-like cavity that leads to the freely accessible metal-ion redox center. The bis(molybdopterin guanine dinucleotide) molybdenum cofactor of the single chain protein has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center
-
oxidized Mo(VI)-form, to 3.5 A resolution. Presence of a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states
-
x-ray absorption spectroscopy study. Dimethyl sulfoxide reductase reduced with trimethylarsine is structurally analogous to the physiologically relevant dimethyl sulfide reduced dimethyl suldfoxide reductase. These species should be regarded as formal MoIV species with a classical coordination complex of trimethylarsine oxide, with no special structural distortions. The similarity of the trimethylarsine and dimethyl sulfide complexes suggests that the dimethyl sulfide reduced enzyme possesses a classical coordination of DMSO with no special elongation of the S-O bond
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
15 min, inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulated under anaerobic conditions
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A178Q
-
mutation in subunit DmsA. About 1200% of wild-type catalytic efficiency; mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
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
C59S
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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
D95A
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mutation in electron transfer subunit DmsB
D95A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D95K/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D97A
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mutation in electron transfer subunit DmsB
D97A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
DELTAN21
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mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled
G167N
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mutation in subunit DmsA. About 20% of wild-type catalytic efficiency; mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
G190D
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mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
G190V
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mutation in subunit DmsA. About 180% of wild-type catalytic efficiency
H106A
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mutation in electron transfer subunit DmsB
H106A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106E
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mutation in electron transfer subunit DmsB
H106E/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106I/C102S 2
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H65R
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mutation in subunit DmsC. Mutant blocks binding of the menaquinol analogue 2-n-heptyl-4-hydroxyquinoline-N-oxide to the protein
H85F
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mutation in electron transfer subunit DmsB
H85F/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H85T
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mutation in electron transfer subunit DmsB
H85T/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
K77A
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mutation in electron transfer subunit DmsB
K77A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
M147I
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mutation in subunit DmsA. About 65% of wild-type catalytic efficiency
M147L
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mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
P80A
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mutation in electron transfer subunit DmsB
P80A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
P80D
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mutation in electron transfer subunit DmsB
P80H
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mutation in electron transfer subunit DmsB
Q179I
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mutation in subunit DmsA. About 500% of wild-type catalytic efficiency; mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
R103A
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mutation in electron transfer subunit DmsB
R103A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
R149C
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mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
R217Q
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mutation in subunit DmsA. About 2.7% of wild-type catalytic efficiency; mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
R61K
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molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity
R77S
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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
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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
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mutation in electron transfer subunit DmsB
S81H
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mutation in electron transfer subunit DmsB
T148S
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mutation in subunit DmsA. About 150% of wild-type catalytic efficiency; mutation in subunit DmsA. Mutant shows altered kinetic parameters for pyridine N-oxide and dimethylsulfoxide, with Km and kcat decreasing and increasing approximately fourfold,respectively
V20Y/DELTAN21/P27G
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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
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addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion
W191G
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mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
W357C
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mutation in subunit DmsA. About 100% of wild-type catalytic efficiency
W357F
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mutation in subunit DmsA. About 40% of wild-type catalytic efficiency
W357Y
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mutation in subunit DmsA. About 60% of wild-type catalytic efficiency
Y104A
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mutation in electron transfer subunit DmsB
Y104A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104D
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mutation in electron transfer subunit DmsB
Y104D/C102S
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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
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104E 
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mutation in electron transfer subunit DmsB
Y104E/C102S
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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
W116F
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residue W116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affects the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm
Y114A
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mutation in direction of the active site of trimethylamine-N-oxide reduxtase. Mutation results in decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide
Y114F
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mutation in direction of the active site of tiomethylamine-N-oxide reduxtase. Mutation results in decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide
additional information
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