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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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discounted EARLY registration ends Dec 31, 2014
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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 terminal electron transfer enzyme, catalyzing a step in an energy-transducing anaerobic electron transport chain. It reduces many other amine-N-oxides and methyl-sulfoxides, including trimethylamine N-oxide (TMAO), but is genetically distinct from other TMAO reductases [Cammack90, Sambasivarao91]. The enzyme contains a molybdenum cofactor, and four iron-sulfur clusters [Weiner88, Cammack90, Trieber94].

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].

Locations [Comment 1]: inner membrane, cytosol

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Cotter89]
GO:0006810 - transport Inferred by computational analysis [GOA00]
Molecular Function: GO:0009389 - dimethyl sulfoxide reductase activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0005829 - cytosol
GO:0005886 - plasma membrane
GO:0016020 - membrane Inferred by computational analysis [GOA00]

Credits:
Reviewed in EcoCyc 16-Apr-2008 by Nolan L , Macquarie University
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: dimethyl sulfoxide reductase

Synonyms: DMSO reductase

EC Number: 1.8.5.3

Alternative Substrates for dimethyl sulfoxide [Comment 2 ]: adenosine-N1-oxide [Weiner88 ] , pyridine-N-oxide [Weiner88 ] , nicotinic acid N-oxide [Weiner88 ] , picolinic 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 , methyl phenyl sulfoxide , phenyl sulfoxide , hydroxylamine , chlorate

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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
The representation of the DMSO reductase complex indiates transfer of protons across the membrane where protons from MQH2 are moved from the cytoplasmic side to the periplasmic side of the cytoplasmic membrane. This representation has not been experimentally established and is therefore speculative.

Cofactors or Prosthetic Groups: Mo2+

Activators (Unknown Mechanism): Fe2+ [Weiner88]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
dimethyl sulfoxide
180.0
79.9
[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 [UniProtGOA11, GOA01]
Molecular Function: GO:0005506 - iron ion binding Inferred from experiment [Rothery91]
GO:0005515 - protein binding Inferred from experiment [Chan10, Chan09, Kostecki10]
GO:0009055 - electron carrier activity Inferred from experiment Inferred by computational analysis [GOA01, Trieber94]
GO:0030151 - molybdenum ion binding Inferred from experiment Inferred by computational analysis [GOA01, Rothery91]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Rothery91]
GO:0009389 - dimethyl sulfoxide reductase activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01, Gaudet10]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, 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:
This subunit contains the active site and the molybdenum cofactor [Rothery91].

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 [Bilous88, Sambasivarao00].


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

Synonyms: DmsB

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

Locations: inner 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 [UniProtGOA11]
Molecular Function: GO:0005506 - iron ion binding Inferred from experiment [Rothery91]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, Rothery91]
GO:0009389 - dimethyl sulfoxide reductase activity Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0005886 - plasma membrane
GO:0016020 - membrane Inferred by computational analysis [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:
This subunit contains four 4Fe-4S clusters and carries out the electron-transfer process. [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 [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0009389 - dimethyl sulfoxide reductase activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Zhang07, Daley05, Weiner93]
GO:0009390 - dimethyl sulfoxide reductase complex Inferred from experiment [Weiner88]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, GOA01, Bilous88]

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:
This subunit anchors the A and B subunits to the membrane and stabilizes the catalytic subunits [Rothery91, Bilous88]. A glutamate residue, E87, was found to be important for menaquinol binding and oxidation [Geijer04].


References

Bairoch93: Bairoch A, Boeckmann B (1993). "The SWISS-PROT protein sequence data bank, recent developments." Nucleic Acids Res. 21:3093-3096. PMID: 8332529

Bilous88: 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

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

Cammack90: Cammack R, Weiner JH (1990). "Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli." Biochemistry 1990;29(36);8410-6. PMID: 2174699

Chan09: Chan CS, Chang L, Rommens KL, Turner RJ (2009). "Differential Interactions between Tat-specific redox enzyme peptides and their chaperones." J Bacteriol 191(7);2091-101. PMID: 19151138

Chan10: Chan CS, Chang L, Winstone TM, Turner RJ (2010). "Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates." FEBS Lett 584(22);4553-8. PMID: 20974141

Cotter89: Cotter PA, Gunsalus RP (1989). "Oxygen, nitrate, and molybdenum regulation of dmsABC gene expression in Escherichia coli." J Bacteriol 171(7);3817-23. PMID: 2544558

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

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."

GOA01: 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

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

Sambasivarao00: Sambasivarao D, Turner RJ, Simala-Grant JL, Shaw G, Hu J, Weiner JH (2000). "Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide reductase of Escherichia coli." J Biol Chem 275(29);22526-31. PMID: 10801884

Sambasivarao90: Sambasivarao D, Scraba DG, Trieber C, Weiner JH (1990). "Organization of dimethyl sulfoxide reductase in the plasma membrane of Escherichia coli." J Bacteriol 1990;172(10);5938-48. PMID: 2170332

Sambasivarao91: Sambasivarao D, Weiner JH (1991). "Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation." J Bacteriol 1991;173(19);5935-43. PMID: 1917829

SimalaGrant96: Simala-Grant JL, Weiner JH (1996). "Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase." Microbiology 142 ( Pt 11);3231-9. PMID: 8969520

Trieber94: Trieber CA, Rothery RA, Weiner JH (1994). "Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coli." J Biol Chem 1994;269(10);7103-9. PMID: 8125918

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Weiner88: Weiner JH, MacIsaac DP, Bishop RE, Bilous PT (1988). "Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity." J Bacteriol 1988;170(4);1505-10. PMID: 3280546

Weiner93: Weiner JH, Shaw G, Turner RJ, Trieber CA (1993). "The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli." J Biol Chem 268(5);3238-44. PMID: 8429002

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111


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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
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc12.