Escherichia coli K-12 substr. MG1655 Enzyme: superoxide dismutase (Mn)

Gene: sodA Accession Numbers: EG10953 (EcoCyc), b3908, ECK3901

Regulation Summary Diagram: ?

Regulation summary diagram for sodA

Subunit composition of superoxide dismutase (Mn) = [SodA]2

SodA, or MnSOD, is one of three superoxide dismutases in E. coli [Britton77]. The three enzymes differ in their metal cofactor requirement; MnSOD contains manganese. Superoxide dismutase is implicated in the response to a large number of environmental changes that lead to the generation of superoxide radicals.

MnSOD and the iron-containing enzyme FeSOD (SodB) are not functionally equivalent; MnSOD is more effective than FeSOD in preventing damage to DNA, while FeSOD seems more effective in protecting a cytoplasmic superoxide-sensitive enzyme [Hopkin92]. However, both enzymes were shown to protect dihydroxy acid dehydratase from inactivation by oxidative stress [Brown95a]. MnSOD binds DNA non-specifically [Steinman94]. The superoxide dismutases contribute to reducing iron toxicity [Touati95].

The enzyme is highly specific for the manganese cofactor; an iron-substituted MnSOD is catalytically inactive [Vance98]. The binding constant for Mn(II) is 3.2 x 108 M-1 [Mizuno04], and the process of manganese acquisition has been studied [Whittaker06]. Metal uptake appears to be cooperative and requires dimer dissociation [Whittaker11]. The Glu170 residue is essential for metal selectivity and is thought to form a hydrogen bond with His171 of the second monomer in the homodimeric enzyme [Whittaker98]. A Gly165Thr mutation confers some activity using Fe as the metal cofactor [Osawa10]. Crystal structures of wild type and mutant apo- and MnSOD have been solved [Edwards98, Borgstahl00, Edwards01, Edwards01a, Porta10, Whittaker11]. The catalytic mechanism and involvement of the metal cofactor have been studied [Vance01, Han02, Maliekal02, Jackson04a, Jackson04b, Jackson05, Tabares05, Tabares06].

Superoxide dismutase is also part of the ribonucleoside-diphosphate reductase activating system. The system is composed of three proteins, flavin reductase, superoxide dismutase and a protein fraction named fraction b whose function is poorly defined [Eliasson86, Fontecave87]. MnSOD was identified as the enzyme present in the system [Eliasson86], but other species of the enzyme could substitute [Coves95].

Production of MnSOD is not dependent on the SOS system [Hancock85]. The complex transcriptional and post-transcriptional regulation of sodA expression has been studied in detail [Touati88, Niederhoffer90a, Niederhoffer90, Naik90, Tardat91, Hassan92, Schrum92, Compan93, Privalle93, Privalle93a, Bowen93, Gardner93, Tardat93, Beaumont93, Schrum93, Schrum94, Schrum94a, Presutti95, Jair96, Jair96a, Tang02, Boysen10, Durand10, Argaman12].

An sodA mutant is more sensitive to paraquat than wild type [Carlioz86] and shows an increased mutation rate that is dependent on the presence of oxygen [Farr86]. A sodA sodB double mutant is especially sensitive to DNA damage induced by hydrogen peroxide [Imlay87]. Under aerobic conditions, a sodA sodB double mutant is able to grow slowly on rich medium, but not on minimal glucose medium. The double mutant is able to grow under anaerobic conditions or by supplementing the minimal medium with a full complement of amino acids [Carlioz86]. The amino acid auxotrophic phenotypes can be explained by oxidative inactivation of dihydroxy acid dehydratase [Brown95a] and transketolase [Benov99]. A sodA sodB double mutant is more susceptible to killing by human serum and neutrophils [McManus95].

Reviews: [Fee91, Hassan94, Whittaker03, Perry10, Miller12, Aguirre12]

Citations: [Gardner87, Privalle88, Privalle89, Privalle90, Privalle92, Lin10a, Kahrstrom12]

Gene Citations: [Takeda86]

Locations: cytosol

Map Position: [4,098,833 -> 4,099,453] (88.34 centisomes, 318°)
Length: 621 bp / 206 aa

Molecular Weight of Polypeptide: 23.097 kD (from nucleotide sequence), 24.0 kD (experimental) [Eliasson86 ]

Molecular Weight of Multimer: 45.0 kD (experimental) [Eliasson86]

pI: 6.88

Isozyme Sequence Similarity:

Unification Links: ASAP:ABE-0012761 , CGSC:17593 , EchoBASE:EB0946 , EcoGene:EG10953 , EcoliWiki:b3908 , ModBase:P00448 , OU-Microarray:b3908 , PortEco:sodA , PR:PRO_000023964 , Pride:P00448 , Protein Model Portal:P00448 , RefSeq:NP_418344 , RegulonDB:EG10953 , SMR:P00448 , String:511145.b3908 , UniProt:P00448

Relationship Links: InterPro:IN-FAMILY:IPR001189 , InterPro:IN-FAMILY:IPR019831 , InterPro:IN-FAMILY:IPR019832 , InterPro:IN-FAMILY:IPR019833 , Panther:IN-FAMILY:PTHR11404 , PDB:Structure:1D5N , PDB:Structure:1EN4 , PDB:Structure:1EN5 , PDB:Structure:1EN6 , PDB:Structure:1I08 , PDB:Structure:1I0H , PDB:Structure:1MMM , PDB:Structure:1VEW , PDB:Structure:1IX9 , PDB:Structure:1IXB , PDB:Structure:1ZLZ , PDB:Structure:3K9S , PDB:Structure:3OT7 , Pfam:IN-FAMILY:PF00081 , Pfam:IN-FAMILY:PF02777 , Prints:IN-FAMILY:PR01703 , Prosite:IN-FAMILY:PS00088

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for sodA

GO Terms:

Biological Process: GO:0006801 - superoxide metabolic process Inferred from experiment Inferred by computational analysis [GOA01a, Gregory73]
GO:0006979 - response to oxidative stress Inferred from experiment [Touati95]
GO:0009408 - response to heat Inferred from experiment [Benov95]
GO:0010447 - response to acidic pH Inferred from experiment [BrunoBarcena10]
GO:0019430 - removal of superoxide radicals Inferred from experiment [Beauchamp71]
GO:0055114 - oxidation-reduction process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Beauchamp71]
GO:0071291 - cellular response to selenium ion Inferred from experiment [Bebien02]
Molecular Function: GO:0003677 - DNA binding Inferred from experiment [Steinman94]
GO:0004784 - superoxide dismutase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Britton77, Beauchamp71, Keele70]
GO:0016209 - antioxidant activity Inferred from experiment [Carlioz86]
GO:0030145 - manganese ion binding Inferred from experiment [Whittaker97, Vance98]
GO:0042803 - protein homodimerization activity Inferred from experiment [Eliasson86]
GO:0046872 - metal ion binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Keele70]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment [Gregroy73, Britton77]
GO:0005829 - cytosol Inferred from experiment [Ishihama08, Britton77]

MultiFun Terms: cell processes protection detoxification

Essentiality data for sodA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Last-Curated ? 04-Dec-2012 by Keseler I , SRI International

Enzymatic reaction of: superoxide dismutase

Synonyms: mangano superoxide dismutase, MnSOD superoxide:superoxide oxidoreductase

EC Number:

2 superoxide + 2 H+ <=> hydrogen peroxide + oxygen

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Alternative Substrates for superoxide: nitric oxide [Filipovic07 ]

In Pathways: superoxide radicals degradation

The enzyme was originally purified from E. coli B [Keele70, Gregory73, Gregroy73].

Cofactors or Prosthetic Groups: Mn2+ [Whittaker97]

Cofactor Binding Comment: contains 1.6-1.8 atoms of Mn per molecule of enzyme [Keele70]

Inhibitors (Unknown Mechanism): azide [Misra78, Tabares06, Comment 5]

Sequence Features

Protein sequence of SodA with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Pasquali94, Steinman78, Link97, UniProt12b]
UniProt: Removed.
Chain 2 -> 206
UniProt: Superoxide dismutase [Mn];
Metal-Binding-Site 27
UniProt: Manganese.
Sequence-Conflict 81 -> 82
[GarciaMartin92, UniProt10]
UniProt: (in Ref. 6);
Metal-Binding-Site 82
UniProt: Manganese.
Acetylation-Modification 114
Acetylation-Modification 119
Extrinsic-Sequence-Variant 165
UniProt: In strain: B..
Metal-Binding-Site 168
UniProt: Manganese.
Metal-Binding-Site 172
UniProt: Manganese.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b3908 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10953; confirmed by SwissProt match.


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Bebien02: Bebien M, Lagniel G, Garin J, Touati D, Vermeglio A, Labarre J (2002). "Involvement of superoxide dismutases in the response of Escherichia coli to selenium oxides." J Bacteriol 184(6);1556-64. PMID: 11872706

Benov95: Benov L, Fridovich I (1995). "Superoxide dismutase protects against aerobic heat shock in Escherichia coli." J Bacteriol 177(11);3344-6. PMID: 7768839

Benov99: Benov L, Fridovich I (1999). "Why superoxide imposes an aromatic amino acid auxotrophy on Escherichia coli. The transketolase connection." J Biol Chem 274(7);4202-6. PMID: 9933617

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Brown95a: Brown OR, Smyk-Randall E, Draczynska-Lusiak B, Fee JA (1995). "Dihydroxy-acid dehydratase, a [4Fe-4S] cluster-containing enzyme in Escherichia coli: effects of intracellular superoxide dismutase on its inactivation by oxidant stress." Arch Biochem Biophys 319(1);10-22. PMID: 7771772

BrunoBarcena10: Bruno-Barcena JM, Azcarate-Peril MA, Hassan HM (2010). "Role of antioxidant enzymes in bacterial resistance to organic acids." Appl Environ Microbiol 76(9);2747-53. PMID: 20305033

Carlioz86: Carlioz A, Touati D (1986). "Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life?." EMBO J 5(3);623-30. PMID: 3011417

Compan93: Compan I, Touati D (1993). "Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12." J Bacteriol 175(6);1687-96. PMID: 8449876

Coves95: Coves J, Delon B, Climent I, Sjoberg BM, Fontecave M (1995). "Enzymic and chemical reduction of the iron center of the Escherichia coli ribonucleotide reductase protein R2. The role of the C-terminus." Eur J Biochem 1995;233(1);357-63. PMID: 7588767

Durand10: Durand S, Storz G (2010). "Reprogramming of anaerobic metabolism by the FnrS small RNA." Mol Microbiol 75(5);1215-31. PMID: 20070527

Edwards01: Edwards RA, Whittaker MM, Whittaker JW, Baker EN, Jameson GB (2001). "Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase." Biochemistry 40(1);15-27. PMID: 11141052

Edwards01a: Edwards RA, Whittaker MM, Whittaker JW, Baker EN, Jameson GB (2001). "Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity." Biochemistry 40(15);4622-32. PMID: 11294629

Edwards98: Edwards RA, Baker HM, Whittaker MM, Whittaker JW, Jameson GB, Baker EN (1998). "Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-Å resolution." J Biol Inorg Chem 3:161-171.

Eliasson86: Eliasson R, Jornvall H, Reichard P (1986). "Superoxide dismutase participates in the enzymatic formation of the tyrosine radical of ribonucleotide reductase from Escherichia coli." Proc Natl Acad Sci U S A 1986;83(8);2373-7. PMID: 3517866

Farr86: Farr SB, D'Ari R, Touati D (1986). "Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase." Proc Natl Acad Sci U S A 83(21);8268-72. PMID: 3022287

Fee91: Fee JA (1991). "Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function." Mol Microbiol 5(11);2599-610. PMID: 1779751

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Filipovic07: Filipovic MR, Stanic D, Raicevic S, Spasic M, Niketic V (2007). "Consequences of MnSOD interactions with nitric oxide: nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide." Free Radic Res 41(1);62-72. PMID: 17164179

Fontecave87: Fontecave M, Eliasson R, Reichard P (1987). "NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase." J Biol Chem 1987;262(25);12325-31. PMID: 3305505

GarciaMartin92: Garcia-Martin C, Baldoma L, Badia J, Aguilar J (1992). "Nucleotide sequence of the rhaR-sodA interval specifying rhaT in Escherichia coli." J Gen Microbiol 138(6);1109-16. PMID: 1339463

Gardner87: Gardner PR, Fridovich I (1987). "Controls on the biosynthesis of the manganese-containing superoxide dismutase of Escherichia coli. Effects of thiols." J Biol Chem 262(36);17591-5. PMID: 3320044

Gardner93: Gardner PR, Fridovich I (1993). "NADPH inhibits transcription of the Escherichia coli manganese superoxide dismutase gene (sodA) in vitro." J Biol Chem 268(17);12958-63. PMID: 8509428

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

Gregory73: Gregory EM, Fridovich I (1973). "Induction of superoxide dismutase by molecular oxygen." J Bacteriol 114(2);543-8. PMID: 4196244

Gregroy73: Gregroy EM, Yost FJ, Fridovich I (1973). "Superoxide dismutases of Escherichia coli: intracellular localization and functions." J Bacteriol 115(3);987-91. PMID: 4580575

Han02: Han WG, Lovell T, Noodleman L (2002). "Coupled redox potentials in manganese and iron superoxide dismutases from reaction kinetics and density functional/electrostatics calculations." Inorg Chem 41(2);205-18. PMID: 11800609

Hancock85: Hancock LC, Hassan HM (1985). "Regulation of the manganese-containing superoxide dismutase is independent of the inducible DNA repair system in Escherichia coli." J Biol Chem 260(24);12954-6. PMID: 2997150

Hassan92: Hassan HM, Sun HC (1992). "Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli." Proc Natl Acad Sci U S A 89(8);3217-21. PMID: 1565612

Hassan94: Hassan HM, Schrum LW (1994). "Roles of manganese and iron in the regulation of the biosynthesis of manganese-superoxide dismutase in Escherichia coli." FEMS Microbiol Rev 14(4);315-23. PMID: 7917419

Hopkin92: Hopkin KA, Papazian MA, Steinman HM (1992). "Functional differences between manganese and iron superoxide dismutases in Escherichia coli K-12." J Biol Chem 1992;267(34);24253-8. PMID: 1447175

Hunter02: Hunter T, Bannister JV, Hunter GJ (2002). "Thermostability of manganese- and iron-superoxide dismutases from Escherichia coli is determined by the characteristic position of a glutamine residue." Eur J Biochem 269(21);5137-48. PMID: 12392545

Imlay87: Imlay JA, Linn S (1987). "Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide." J Bacteriol 169(7);2967-76. PMID: 3298208

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jackson04a: Jackson TA, Brunold TC (2004). "Combined spectroscopic/computational studies on Fe- and Mn-dependent superoxide dismutases: insights into second-sphere tuning of active site properties." Acc Chem Res 37(7);461-70. PMID: 15260508

Jackson04b: Jackson TA, Karapetian A, Miller AF, Brunold TC (2004). "Spectroscopic and computational studies of the azide-adduct of manganese superoxide dismutase: definitive assignment of the ligand responsible for the low-temperature thermochromism." J Am Chem Soc 126(39);12477-91. PMID: 15453782

Jackson05: Jackson TA, Karapetian A, Miller AF, Brunold TC (2005). "Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of oxidized manganese superoxide dismutase." Biochemistry 44(5);1504-20. PMID: 15683235

Jair96: Jair KW, Fawcett WP, Fujita N, Ishihama A, Wolf RE (1996). "Ambidextrous transcriptional activation by SoxS: requirement for the C-terminal domain of the RNA polymerase alpha subunit in a subset of Escherichia coli superoxide-inducible genes." Mol Microbiol 1996;19(2);307-17. PMID: 8825776

Jair96a: Jair KW, Yu X, Skarstad K, Thony B, Fujita N, Ishihama A, Wolf RE (1996). "Transcriptional activation of promoters of the superoxide and multiple antibiotic resistance regulons by Rob, a binding protein of the Escherichia coli origin of chromosomal replication." J Bacteriol 1996;178(9);2507-13. PMID: 8626315

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kahrstrom12: Kahrstrom CT (2012). "Cellular microbiology: Ironing out Hfq regulation." Nat Rev Microbiol 10(5);310-1. PMID: 22450378

Keele70: Keele BB, McCord JM, Fridovich I (1970). "Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme." J Biol Chem 1970;245(22);6176-81. PMID: 4921969

Lin10a: Lin CN, Syu WJ, Sun WS, Chen JW, Chen TH, Don MJ, Wang SH (2010). "A role of ygfZ in the Escherichia coli response to plumbagin challenge." J Biomed Sci 17;84. PMID: 21059273

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

Maliekal02: Maliekal J, Karapetian A, Vance C, Yikilmaz E, Wu Q, Jackson T, Brunold TC, Spiro TG, Miller AF (2002). "Comparison and contrasts between the active site PKs of Mn-superoxide dismutase and those of Fe-superoxide dismutase." J Am Chem Soc 124(50);15064-75. PMID: 12475351

McManus95: McManus DC, Josephy PD (1995). "Superoxide dismutase protects Escherichia coli against killing by human serum." Arch Biochem Biophys 317(1);57-61. PMID: 7872803

Miller12: Miller AF (2012). "Superoxide dismutases: ancient enzymes and new insights." FEBS Lett 586(5);585-95. PMID: 22079668

Misra78: Misra HP, Fridovich I (1978). "Inhibition of superoxide dismutases by azide." Arch Biochem Biophys 1978;189(2);317-22. PMID: 213023

Mizuno04: Mizuno K, Whittaker MM, Bachinger HP, Whittaker JW (2004). "Calorimetric studies on the tight binding metal interactions of Escherichia coli manganese superoxide dismutase." J Biol Chem 279(26);27339-44. PMID: 15082717

Naik90: Naik SM, Hassan HM (1990). "Use of site-directed mutagenesis to identify an upstream regulatory sequence of sodA gene of Escherichia coli K-12." Proc Natl Acad Sci U S A 87(7);2618-22. PMID: 2181443

Niederhoffer90: Niederhoffer EC, Naranjo CM, Bradley KL, Fee JA (1990). "Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus." J Bacteriol 172(4);1930-8. PMID: 2180912

Niederhoffer90a: Niederhoffer EC, Fee JA (1990). "Novel effect of aromatic compounds on the iron-dependent expression of the Escherichia coli K12 manganese superoxide dismutase (sodA) gene." Biol Met 3(3-4);237-41. PMID: 2127370

Osawa10: Osawa M, Yamakura F, Mihara M, Okubo Y, Yamada K, Hiraoka BY (2010). "Conversion of the metal-specific activity of Escherichia coli Mn-SOD by site-directed mutagenesis of Gly165Thr." Biochim Biophys Acta 1804(9);1775-9. PMID: 20451673

Pasquali94: Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. (1994). Data submission to UniProtKB on 1994-09.

Perry10: Perry JJ, Shin DS, Getzoff ED, Tainer JA (2010). "The structural biochemistry of the superoxide dismutases." Biochim Biophys Acta 1804(2);245-62. PMID: 19914407

Porta10: Porta J, Vahedi-Faridi A, Borgstahl GE (2010). "Structural analysis of peroxide-soaked MnSOD crystals reveals side-on binding of peroxide to active-site manganese." J Mol Biol 399(3);377-84. PMID: 20417642

Presutti95: Presutti DG, Hassan HM (1995). "Binding of integration host factor (IHF) to the Escherichia coli sodA gene and its role in the regulation of a sodA-lacZ fusion gene." Mol Gen Genet 1995;246(2);228-35. PMID: 7862094

Privalle88: Privalle CT, Fridovich I (1988). "Inductions of superoxide dismutases in Escherichia coli under anaerobic conditions. Accumulation of an inactive form of the manganese enzyme." J Biol Chem 263(9);4274-9. PMID: 3279033

Privalle89: Privalle CT, Beyer WF, Fridovich I (1989). "Anaerobic induction of ProMn-superoxide dismutase in Escherichia coli." J Biol Chem 264(5);2758-63. PMID: 2644272

Privalle90: Privalle CT, Fridovich I (1990). "Anaerobic biosynthesis of the manganese-containing superoxide dismutase in Escherichia coli. Effects of diazenedicarboxylic acid bis(N,N'-dimethylamide) (diamide)." J Biol Chem 265(35);21966-70. PMID: 2254340

Privalle92: Privalle CT, Fridovich I (1992). "Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese-superoxide dismutase in Escherichia coli." J Biol Chem 267(13);9140-5. PMID: 1577750

Privalle93: Privalle CT, Fridovich I (1993). "Iron specificity of the Fur-dependent regulation of the biosynthesis of the manganese-containing superoxide dismutase in Escherichia coli." J Biol Chem 268(7);5178-81. PMID: 8444893

Privalle93a: Privalle CT, Kong SE, Fridovich I (1993). "Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: sites of transcriptional regulation." Proc Natl Acad Sci U S A 90(6);2310-4. PMID: 8460139

Schrum92: Schrum LW, Hassan HM (1992). "Transcriptional regulation of Mn-superoxide dismutase gene (sodA) of Escherichia coli is stimulated by DNA gyrase inhibitors." Arch Biochem Biophys 299(1);185-92. PMID: 1332615

Schrum93: Schrum LW, Hassan HM (1993). "Transcriptional activation of Mn-superoxide dismutase gene (sodA) of Escherichia coli by MnCl2." Biochim Biophys Acta 1216(2);186-90. PMID: 8241258

Schrum94: Schrum LW, Hassan HM (1994). "The effects of fur on the transcriptional and post-transcriptional regulation of MnSOD gene (sodA) in Escherichia coli." Arch Biochem Biophys 309(2);288-92. PMID: 8135540

Schrum94a: Schrum LW, Hassan HM (1994). "Stability of Escherichia coli sodA mRNA and identification of the transcriptional start site(s) under different environmental and oxidative stresses." Free Radic Biol Med 17(3);209-13. PMID: 7982626

Steinman78: Steinman HM (1978). "The amino acid sequence of mangano superoxide dismutase from Escherichia coli B." J Biol Chem 253(24);8708-20. PMID: 363708

Steinman94: Steinman HM, Weinstein L, Brenowitz M (1994). "The manganese superoxide dismutase of Escherichia coli K-12 associates with DNA." J Biol Chem 269(46);28629-34. PMID: 7961811

Tabares05: Tabares LC, Cortez N, Agalidis I, Un S (2005). "Temperature-dependent coordination in E. coli manganese superoxide dismutase." J Am Chem Soc 127(16);6039-47. PMID: 15839704

Tabares06: Tabares LC, Cortez N, Hiraoka BY, Yamakura F, Un S (2006). "Effects of substrate analogues and pH on manganese superoxide dismutases." Biochemistry 45(6);1919-29. PMID: 16460038

Takeda86: Takeda Y, Avila H (1986). "Structure and gene expression of the E. coli Mn-superoxide dismutase gene." Nucleic Acids Res 14(11);4577-89. PMID: 3520487

Tang02: Tang Y, Quail MA, Artymiuk PJ, Guest JR, Green J (2002). "Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression." Microbiology 148(Pt 4);1027-37. PMID: 11932448

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Other References Related to Gene Regulation

Ariza95: Ariza RR, Li Z, Ringstad N, Demple B (1995). "Activation of multiple antibiotic resistance and binding of stress-inducible promoters by Escherichia coli Rob protein." J Bacteriol 1995;177(7);1655-61. PMID: 7896685

Baez13a: Baez A, Shiloach J (2013). "Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase." Microb Cell Fact 12;23. PMID: 23497217

Chen07: Chen Z, Lewis KA, Shultzaberger RK, Lyakhov IG, Zheng M, Doan B, Storz G, Schneider TD (2007). "Discovery of Fur binding site clusters in Escherichia coli by information theory models." Nucleic Acids Res 35(20);6762-77. PMID: 17921503

Fawcett95: Fawcett WP, Wolf RE (1995). "Genetic definition of the Escherichia coli zwf "soxbox," the DNA binding site for SoxS-mediated induction of glucose 6-phosphate dehydrogenase in response to superoxide." J Bacteriol 1995;177(7);1742-50. PMID: 7896696

Iuchi94: Iuchi S, Aristarkhov A, Dong JM, Taylor JS, Lin EC (1994). "Effects of nitrate respiration on expression of the Arc-controlled operons encoding succinate dehydrogenase and flavin-linked L-lactate dehydrogenase." J Bacteriol 1994;176(6);1695-701. PMID: 8132465

Jair95: Jair KW, Martin RG, Rosner JL, Fujita N, Ishihama A, Wolf RE (1995). "Purification and regulatory properties of MarA protein, a transcriptional activator of Escherichia coli multiple antibiotic and superoxide resistance promoters." J Bacteriol 1995;177(24);7100-4. PMID: 8522515

Kumar11: Kumar R, Shimizu K (2011). "Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures." Microb Cell Fact 10;3. PMID: 21272324

Liu04: Liu X, De Wulf P (2004). "Probing the ArcA-P modulon of Escherichia coli by whole genome transcriptional analysis and sequence recognition profiling." J Biol Chem 279(13);12588-97. PMID: 14711822

Lu03a: Lu C, Bentley WE, Rao G (2003). "Comparisons of oxidative stress response genes in aerobic Escherichia coli fermentations." Biotechnol Bioeng 83(7);864-70. PMID: 12889026

Martin11: Martin RG, Rosner JL (2011). "Promoter discrimination at class I MarA regulon promoters mediated by glutamic acid 89 of the MarA transcriptional activator of Escherichia coli." J Bacteriol 193(2);506-15. PMID: 21097628

Martin99: Martin RG, Gillette WK, Rhee S, Rosner JL (1999). "Structural requirements for marbox function in transcriptional activation of mar/sox/rob regulon promoters in Escherichia coli: sequence, orientation and spatial relationship to the core promoter." Mol Microbiol 1999;34(3);431-41. PMID: 10564485

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

Pomposiello01: Pomposiello PJ, Bennik MH, Demple B (2001). "Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate." J Bacteriol 183(13);3890-902. PMID: 11395452

Varghese07: Varghese S, Wu A, Park S, Imlay KR, Imlay JA (2007). "Submicromolar hydrogen peroxide disrupts the ability of Fur protein to control free-iron levels in Escherichia coli." Mol Microbiol 64(3);822-30. PMID: 17462026

Via96: Via P, Badia J, Baldoma L, Obradors N, Aguilar J (1996). "Transcriptional regulation of the Escherichia coli rhaT gene." Microbiology 1996;142 ( Pt 7);1833-40. PMID: 8757746

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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