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MetaCyc Enzyme: dimethyl sulfoxide reductase

Synonyms: DMSO/TMAO reductase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of dimethyl sulfoxide reductase = [DmsA][DmsB][DmsC]
         dimethyl sulfoxide reductase, chain A = DmsA (summary available)
         dimethyl sulfoxide reductase, chain B = DmsB (summary available)
         dimethyl sulfoxide reductase, chain C = DmsC (summary available)

Summary:
Dimethyl sulfoxide (DMSO) reductase is a membrane-associated Fe-S molybdoenzyme which catalyses the reduction of DMSO to dimethyl sulfide. The enzyme functions as a terminal reductase during anaerobic respiration on DMSO [Bilous85, Bilous88, Sambasivarao91]. Purified DMSO reductase has broad substrate specificity - it is active on hydroxylamine and chlorate plus a range of amine-N-oxides (including trimethylamine N-oxide ) and methyl-sulfoxides [Weiner88].

DMSO reductase is a member of the complex iron sulfur molybdoenzyme (CISM) family [Rothery08]. The enzyme complex contains three non-identical subunits - a catalytic subunit (DmsA) with a molybdo-bis(pyranopterin guanine dinucleotide) (Mo-bisPGD) cofactor and a [4Fe-4S] cluster (known as FS0), an electron transfer subunit (DmsB) containing four [4Fe-4S] clusters (FS1-FS4) and a membrane anchor subunit (DmsC) containing the quinone-binding site [Weiner88, Cammack90, Trieber94]. Electron transfer is believed to occur from the menaquinol binding site in DmsC, via the Fe-S clusters in DmsB to the site of DMSO reduction in DmsA [Tang11].

Early experiments suggested that the DmsAB subunits were located on the cytoplasmic face of the inner membrane [Sambasivarao91, Rothery93] however later work showed they were present at the the periplasmic face of the inner membrane [Stanley02]. DmsC is the integral membrane subunit - it is required for membrane localization of the complex [Weiner93, Sambasivarao91].

Insertion of the molybdenum cofactor and targeting of the enzyme to the inner membrane requires the redox enzyme maturation protein (REMP), DmsD (reviewed in [Sargent02]).

The enzyme functions anaerobically in the absence of nitrate (a preferred terminal electron acceptor). Anaerobiosis stimulates its expression 100-fold, an effect controlled by the Fnr regulatory protein [Cotter89].

Please note: analysis of DMSO reductase has largely been done using E. coli HB101.

Reviews: [Weiner92]

Citations: [Tang13, Rothery99, Rothery96, Cheng05, SimalaGrant98]

Locations [Comment 1]: inner membrane

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Sambasivarao91, Bilous85, Cotter89]
GO:0019645 - anaerobic electron transport chain Inferred from experiment [Bilous85, Bogachev96]
GO:0006810 - transport Inferred by computational analysis [GOA00]
Molecular Function: GO:0009389 - dimethyl sulfoxide reductase activity Inferred by computational analysis Inferred from experiment [Sambasivarao91, Bilous85, Weiner88, GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment [Sambasivarao91, Weiner88]
GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0031237 - intrinsic component of periplasmic side of plasma membrane Inferred from experiment [Stanley02]
GO:0016020 - membrane Inferred by computational analysis [GOA00]

Credits:
Revised in EcoCyc 04-Nov-2014 by Mackie A , Macquarie University
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Enzymatic reaction of: dimethyl sulfoxide reductase

Synonyms: DMSO reductase

EC Number: 1.8.5.3

Transport reaction diagram for dimethyl sulfoxide reductase

Alternative Substrates for dimethyl sulfoxide [Comment 2 ]: pyridine-N-oxide [Weiner88 ] , nicotinic acid N-oxide [Weiner88 ] , α-picoline N-oxide [Weiner88 ] , hydroxypyridine N-oxide [Weiner88 ] , nicotinamide N-oxide [Weiner88 ] , 3-picoline N-oxide [Weiner88 ] , 4-picoline N-oxide [Weiner88 ] , trimethylamine N-oxide [Weiner88 ] , tetrahydrothiophene 1-oxide [Weiner88 ] , L-methionine S-oxide [Weiner88 ] , methyl phenyl sulfoxide [Weiner88 ] , hydroxylamine [Weiner88 ] , chlorate [Weiner88 ]

In Pathways: formate to dimethyl sulfoxide electron transfer , NADH to dimethyl sulfoxide electron transfer

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International

Cofactors or Prosthetic Groups: a [4Fe-4S] iron-sulfur cluster [Cammack90], bis(guanylyl molybdopterin cofactor) [Tang11]

Activators (Unknown Mechanism): Fe2+ [Weiner88]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
L-methionine S-oxide
470.0
[Weiner88]
nicotinamide N-oxide
500.0
[Weiner88]
chlorate
7750.0
[Weiner88]
tetrahydrothiophene 1-oxide
600.0
[Weiner88]
4-picoline N-oxide
1000.0
[Weiner88]
dimethyl sulfoxide
180.0
79.9
0.44
[SimalaGrant96, BRENDA14]


Subunit of dimethyl sulfoxide reductase: dimethyl sulfoxide reductase, chain A

Synonyms: DmsA

Gene: dmsA Accession Numbers: EG10232 (MetaCyc), b0894, ECK0885

Locations [Comment 3]: inner membrane

Sequence Length: 814 AAs

Molecular Weight: 90.398 kD (from nucleotide sequence)

pI: 6.53

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Cotter89]
GO:0006810 - transport Inferred by computational analysis [GOA00]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Chan10, Chan09, Kostecki10]
GO:0009055 - electron carrier activity Inferred from experiment Inferred by computational analysis [GOA01a, Trieber94]
GO:0009389 - dimethyl sulfoxide reductase activity Inferred from experiment Inferred by computational analysis [GOA01a, Sambasivarao91]
GO:0048037 - cofactor binding Inferred from experiment [Tang11]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Tang11]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a, Gaudet10]
GO:0030151 - molybdenum ion binding Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0031237 - intrinsic component of periplasmic side of plasma membrane Inferred from experiment [Stanley02]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, Gaudet10]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors

Unification Links: DIP:DIP-9452N , EcoliWiki:b0894 , Mint:MINT-8046334 , ModBase:P18775 , PR:PRO_000022455 , Pride:P18775 , Protein Model Portal:P18775 , RefSeq:NP_415414 , SMR:P18775 , String:511145.b0894 , UniProt:P18775

Relationship Links: InterPro:IN-FAMILY:IPR006311 , InterPro:IN-FAMILY:IPR006655 , InterPro:IN-FAMILY:IPR006656 , InterPro:IN-FAMILY:IPR006657 , InterPro:IN-FAMILY:IPR006963 , InterPro:IN-FAMILY:IPR009010 , InterPro:IN-FAMILY:IPR011888 , InterPro:IN-FAMILY:IPR019546 , InterPro:IN-FAMILY:IPR027467 , Pfam:IN-FAMILY:PF00384 , Pfam:IN-FAMILY:PF01568 , Pfam:IN-FAMILY:PF04879 , Prosite:IN-FAMILY:PS00490 , Prosite:IN-FAMILY:PS00551 , Prosite:IN-FAMILY:PS00932 , Prosite:IN-FAMILY:PS51318 , Prosite:IN-FAMILY:PS51669 , Smart:IN-FAMILY:SM00926

Summary:
The DmsA subunit of DMSO reductase contains a molybdo-bis(pyranopterin guanine dinucleotide) (Mo-bisPGD) cofactor and a [4Fe-4S] cluster (known as FS0) [Tang11].

DmsA contains a twin-arginine leader peptide which targets the protein to the membrane, although DmsA does not appear to be exported to the periplasm. The leader peptide is also essential for expression of DmsA and stability of the DmsAB dimer, and is cleaved between residues 45 and 46 [Bilous88a, Sambasivarao00]. The leader peptide interacts with the redox enzyme maturation protein (REMP) DmsD [Oresnik01, Chan08, Winstone13].


Subunit of dimethyl sulfoxide reductase: dimethyl sulfoxide reductase, chain B

Synonyms: DmsB

Gene: dmsB Accession Numbers: EG10233 (MetaCyc), b0895, ECK0886

Locations: membrane

Sequence Length: 205 AAs

Molecular Weight: 22.869 kD (from nucleotide sequence)

pI: 6.79

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Cotter89]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0009389 - dimethyl sulfoxide reductase activity Inferred by computational analysis Inferred from experiment [Weiner88, GOA01a]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Cammack90, Rothery91]
GO:0009055 - electron carrier activity Inferred by computational analysis [Gaudet10]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [Gaudet10]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0031237 - intrinsic component of periplasmic side of plasma membrane Inferred from experiment [Stanley02]
GO:0016020 - membrane Inferred by computational analysis [Gaudet10, GOA00]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors

Unification Links: DIP:DIP-9453N , EcoliWiki:b0895 , ModBase:P18776 , PR:PRO_000022456 , Pride:P18776 , Protein Model Portal:P18776 , RefSeq:NP_415415 , SMR:P18776 , String:511145.b0895 , UniProt:P18776

Relationship Links: InterPro:IN-FAMILY:IPR001450 , InterPro:IN-FAMILY:IPR014297 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , Pfam:IN-FAMILY:PF12797 , Pfam:IN-FAMILY:PF13247 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51379

Summary:
The DmsB subunit of DMSO reductase subunit contains four 4 (4Fe-4S) clusters - FS1, FS2, FS3 and FS4 [Cammack90, Rothery91].


Subunit of dimethyl sulfoxide reductase: dimethyl sulfoxide reductase, chain C

Synonyms: DmsC

Gene: dmsC Accession Numbers: EG10234 (MetaCyc), b0896, ECK0887

Locations [Comment 4]: inner membrane

Sequence Length: 287 AAs

Molecular Weight: 30.826 kD (from nucleotide sequence)

pI: 9.21

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Cotter89]
GO:0006810 - transport Inferred by computational analysis [GOA00]
GO:0019645 - anaerobic electron transport chain Inferred by computational analysis [GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0009389 - dimethyl sulfoxide reductase activity Inferred by computational analysis Inferred from experiment [Weiner88, GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05]
GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis [Weiner93]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a, Bilous88a]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron acceptors

Unification Links: EcoliWiki:b0896 , PR:PRO_000022457 , Protein Model Portal:P18777 , RefSeq:NP_415416 , String:511145.b0896 , UniProt:P18777

Relationship Links: InterPro:IN-FAMILY:IPR007059 , Pfam:IN-FAMILY:PF04976

Summary:
DmsC is the integral membrane subunit of the DMSO reductase complex. It is predicted to have 8 transmembrane helices with the N and C termini located in the periplasm [Weiner93]. This subunit anchors and stabilizes the catalytic subunits DmsA and DmsB [Rothery91, Bilous88a]. A glutamate residue, E87, is important for menaquinol binding and oxidation [Geijer04].


References

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Bilous85: Bilous PT, Weiner JH (1985). "Proton translocation coupled to dimethyl sulfoxide reduction in anaerobically grown Escherichia coli HB101." J Bacteriol 163(1);369-75. PMID: 2989249

Bilous88: Bilous PT, Weiner JH (1988). "Molecular cloning and expression of the Escherichia coli dimethyl sulfoxide reductase operon." J Bacteriol 170(4);1511-8. PMID: 2832366

Bilous88a: Bilous PT, Cole ST, Anderson WF, Weiner JH (1988). "Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli." Mol Microbiol 2(6);785-95. PMID: 3062312

Bogachev96: Bogachev AV, Murtazina RA, Skulachev VP (1996). "H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells." J Bacteriol 178(21);6233-7. PMID: 8892824

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

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Chan08: Chan CS, Winstone TM, Chang L, Stevens CM, Workentine ML, Li H, Wei Y, Ondrechen MJ, Paetzel M, Turner RJ (2008). "Identification of residues in DmsD for twin-arginine leader peptide binding, defined through random and bioinformatics-directed mutagenesis." Biochemistry 47(9);2749-59. PMID: 18247574

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Geijer04: Geijer P, Weiner JH (2004). "Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli." Biochim Biophys Acta 1660(1-2);66-74. PMID: 14757221

GOA00: GOA (2000). "Gene Ontology annotation based on Swiss-Prot keyword mapping."

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Kostecki10: Kostecki JS, Li H, Turner RJ, DeLisa MP (2010). "Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation." PLoS One 5(2);e9225. PMID: 20169075

Oresnik01: Oresnik IJ, Ladner CL, Turner RJ (2001). "Identification of a twin-arginine leader-binding protein." Mol Microbiol 40(2);323-31. PMID: 11309116

Rothery08: Rothery RA, Workun GJ, Weiner JH (2008). "The prokaryotic complex iron-sulfur molybdoenzyme family." Biochim Biophys Acta 1778(9);1897-929. PMID: 17964535

Rothery91: Rothery RA, Weiner JH (1991). "Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis." Biochemistry 1991;30(34);8296-305. PMID: 1653010

Rothery93: Rothery RA, Weiner JH (1993). "Topological characterization of Escherichia coli DMSO reductase by electron paramagnetic resonance spectroscopy of an engineered [3Fe-4S] cluster." Biochemistry 32(22);5855-61. PMID: 8389193

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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