Escherichia coli K-12 substr. MG1655 Enzyme: 2-oxoglutarate decarboxylase, thiamine-requiring

Gene: sucA Accession Numbers: EG10979 (EcoCyc), b0726, ECK0714

Synonyms: lys, lys+met, E1(o) subunit

Regulation Summary Diagram: ?

Regulation summary diagram for sucA

Component of: 2-oxoglutarate dehydrogenase complex (summary available)

Subunit composition of 2-oxoglutarate decarboxylase, thiamine-requiring = [SucA]12
         subunit of E1(0) component of 2-oxoglutarate dehydrogenase = SucA

E. coli SucA is responsible for the 2-oxoglutarate decarboxylase activity of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDHC) that catalyzes the conversion of 2-oxoglutarate (2-ketoglutarate) to succinyl-CoA and CO2, with the production of NADH (see 2-oxoglutarate decarboxylation to succinyl-CoA).

The OGDHC is a member of the 2-oxo acid dehydrogenase family [Bunik08]. Members of this family contain multiple copies of three enzymatic components: 2-oxoglutarate decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). In most Gram-positive bacteria and in mitochondria the E1 component is a heterodimer composed of two subunits, while in most (but not all) Gram-negative bacteria it is made up of a single type of subunit. In both cases multiple copies of the E1 component along with multiple copies of the E3 component are assembled around an E2 core of 24 subunits with octahedral symmetry, or 60 subunits with eicosahedral symmetry (depending on which complex and species) [Reed01]. In E. coli the E3 component is shared with the pyruvate dehydrogenase and glycine cleavage multi-enzyme complexes. E1 and E2 differ slightly for the 2-oxoglutarate and pyruvate dehydrogenase complexes, and are designated (o) and (p) to distinguish them.

The E. coli OGDHC contains 12 units of the E1(o) component 2-oxoglutarate decarboxylase, thiamine-requiring encoded by sucA, 24 units of the E2(o) comoponent dihydrolipoyltranssuccinylase encoded by sucB, and 2 units of the E3 component lipoamide dehydrogenase encoded by lpd. The 24 E2(o) units form the octahedral core of the complex. They contain lipoyllysine and binding sites for dimers of the E1(o) and E3 subunits. Electron cryotomography showed that they are flexibly tethered to the E2 core [Murphy05].

During the OGDHC reaction cycle, 2-oxoglutarate is bound and decarboxylated by SucA, a thiamin-diphosphate cofactor containing enzyme. The crystal structure of a truncated, apo form of SucA lacking the N-terminal 77 residues has been determined at 2.6 Å resolution. The structure of the holo form with thiamin diphoisphate and Mg2+ was determined at 3.5 Å resolution. The truncated form retained decarboxylase activity but did not assemble with E2(o) into an OGDH complex. Data also suggested the presence of an AMP binding site [Frank07]. An oxygen-dependent thiamin free radical was demonstrated in the OGDHC, which was generated by a side reaction with O2 [Frank08].

Studies of engineered SucA prepared by saturation mutagenesis of His260 and His298 suggested that His260 is required for substrate recognition, but His298 could be replaced by hydrophobic residues of similar size. Data also suggested that E2(o) has a role in specificity [Shim11].

REACTION: E1(o) + TPP = E1(o).TPP, E1(o).TPP + 2-oxoglutarate = E1(o).hydroxycarboxypropylTPP + CO(2), E1(o).hydroxycarboxypropylTPP + E2(o).lipoate(S2) = E1(o).TPP + E2(o).lipoate(SH)(S-succinyl) (see [Waskiewicz84, Steginsky85])

The sucA gene was cloned and sequenced in earlier work [Spencer82, Darlison84] and regulation of sucABCD was studied [Park97, Cunningham98]. The sucAB and sucCD genes were shown to be mutually essential, with either pair sufficient to produce succinyl-CoA, but simultaneous deletion of sucAB and sucCD was not viable [Yu06].

Reviews: [Reed74, Perham87, Perham89, Perham00, Reed01, Perham02]

Gene Citations: [Spencer85, Wood84, Magnusson86, Buck86, Buck89]

Locations: cytosol

Map Position: [757,929 -> 760,730] (16.34 centisomes, 59°)
Length: 2802 bp / 933 aa

Molecular Weight of Polypeptide: 105.06 kD (from nucleotide sequence)

pI: 6.42

Unification Links: ASAP:ABE-0002478 , CGSC:146 , DIP:DIP-36225N , EchoBASE:EB0972 , EcoGene:EG10979 , EcoliWiki:b0726 , Mint:MINT-1243484 , ModBase:P0AFG3 , OU-Microarray:b0726 , PortEco:sucA , PR:PRO_000024002 , Pride:P0AFG3 , Protein Model Portal:P0AFG3 , RefSeq:NP_415254 , RegulonDB:EG10979 , SMR:P0AFG3 , String:511145.b0726 , UniProt:P0AFG3

Relationship Links: InterPro:IN-FAMILY:IPR001017 , InterPro:IN-FAMILY:IPR005475 , InterPro:IN-FAMILY:IPR011603 , InterPro:IN-FAMILY:IPR029061 , Panther:IN-FAMILY:PTHR23152 , PDB:Structure:2JGD , Pfam:IN-FAMILY:PF00676 , Pfam:IN-FAMILY:PF02779 , Smart:IN-FAMILY:SM00861

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reactions of [a [lipoyl-carrier protein] N6-dihydrolipoyl-L-lysine + NAD+ = a [lipoyl-carrier protein] N6-lipoyl-L-lysine + NADH + H+] (
i1: a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ → a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+ (

i2: a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ → a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+ (

i3: a [glycine-cleavage complex H protein] N6-dihydrolipoyl-L-lysine + NAD+ ↔ a [glycine-cleavage complex H protein] N6-lipoyl-L-lysine + NADH + H+ (

Genetic Regulation Schematic: ?

Genetic regulation schematic for sucA

GO Terms:

Biological Process: GO:0006096 - glycolytic process Inferred by computational analysis [UniProtGOA11]
GO:0006099 - tricarboxylic acid cycle Inferred by computational analysis [Gaudet10, GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment [Frank07]
GO:0004591 - oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Frank07]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05]
GO:0030976 - thiamine pyrophosphate binding Inferred from experiment Inferred by computational analysis [GOA01, Frank07]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Lasserre06]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
GO:0016624 - oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Lasserre06]
GO:0045252 - oxoglutarate dehydrogenase complex Inferred by computational analysis [Gaudet10]

MultiFun Terms: metabolism energy metabolism, carbon TCA cycle

Essentiality data for sucA knockouts: ?

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

Last-Curated ? 19-Jun-2012 by Fulcher C , SRI International

Enzymatic reaction of: 2-oxoglutarate decarboxylase

Synonyms: oxoglutarate oxidoreductase, decarboxylase, 2-ketoglutarate decarboxylase

EC Number:

2-oxoglutarate + a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine + H+ <=> a [2-oxoglutarate dehydrogenase E2 protein] N6-S-succinyldihydrolipoyl-L-lysine + CO2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: 2-oxoglutarate decarboxylation to succinyl-CoA

E1(o) activity was analyzed by mixing purified E1(o) enzyme with E2(o) and E3 enzymes in vitro and monitoring the formation of NADH spectrophotometrically [Frank07]. The [Waskiewicz84] data are for E. coli B.

Cofactors or Prosthetic Groups: thiamin diphosphate [Frank07, Waskiewicz84], Mg2+ [Frank07, Waskiewicz84]

Inhibitors (Unknown Mechanism): oxaloacetate [Frank07]

Kinetic Parameters:

Km (μM)
[Gupta80, BRENDA14]

pH(opt): 8 [BRENDA14, Gupta79a]

Subunit of: 2-oxoglutarate dehydrogenase complex

Subunit composition of 2-oxoglutarate dehydrogenase complex = [(SucA)12][(SucB)24][(Lpd)2]
         2-oxoglutarate decarboxylase, thiamine-requiring = (SucA)12 (extended summary available)
                 subunit of E1(0) component of 2-oxoglutarate dehydrogenase = SucA
         dihydrolipoyltranssuccinylase = (SucB)24 (extended summary available)
         lipoamide dehydrogenase = (Lpd)2 (extended summary available)
                 E3 monomer = Lpd

The 2-oxoglutarate (2-ketoglutarate) dehydrogenase complex is similar in enzyme composition and complex reactions to the pyruvate dehydrogenase complex reactions [Perham87, Stephens83, Perham89] (see 2-oxoglutarate decarboxylation to succinyl-CoA and pyruvate decarboxylation to acetyl CoA).

SUBREACTIONS: E1(o) + TPP = E1(o).TPP E1(o).TPP + succinate = E1(o).hydroxycarboxypropylTPP + CO(2) E1(o).hydroxycarboxypropylTPP + E2(o).lipoate(S2) = E1(o).TPP + E2(o).lipoate(SH)(S-succinyl) E2(o).lipoate(SH)(S-succinyl) + CoA = E2(o).lip(SH)2 + succinylCoA E3 + FAD = E3.FAD E3.FAD + E2(o).lip(SH)2 = E3.FADH(2) + E2(o).lip(S)2 E3.FADH(2) + NAD(+) = E3.FAD + NADH + H(+) (see [Steginsky85, Waskiewicz84].

Enzymatic reaction of: 2-oxoglutarate dehydrogenase

Synonyms: α-ketoglutarate dehydrogenase, 2-ketoglutarate dehydrogenase

2-oxoglutarate + coenzyme A + NAD+ <=> succinyl-CoA + CO2 + NADH

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: 2-oxoglutarate decarboxylation to succinyl-CoA , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , superpathway of glyoxylate bypass and TCA , TCA cycle I (prokaryotic)

The [Waskiewicz84] data are for E. coli B.

Cofactors or Prosthetic Groups: thiamin diphosphate [Frank07, Waskiewicz84], FAD [Lindsay00], Mg2+ [Frank07, Waskiewicz84]

Sequence Features

Protein sequence of subunit of E1(0) component of 2-oxoglutarate dehydrogenase with features indicated

Feature Class Location Citations Comment
Sequence-Conflict 454
[Darlison84, UniProt10]
UniProt: (in Ref. 1; AAA23897/CAA25280);

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b0726 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10979; confirmed by SwissProt match.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014."

Buck86: Buck D, Spencer ME, Guest JR (1986). "Cloning and expression of the succinyl-CoA synthetase genes of Escherichia coli K12." J Gen Microbiol 1986;132 ( Pt 6);1753-62. PMID: 3543212

Buck89: Buck D, Guest JR (1989). "Overexpression and site-directed mutagenesis of the succinyl-CoA synthetase of Escherichia coli and nucleotide sequence of a gene (g30) that is adjacent to the suc operon." Biochem J 1989;260(3);737-47. PMID: 2548486

Bunik08: Bunik VI, Degtyarev D (2008). "Structure-function relationships in the 2-oxo acid dehydrogenase family: substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins." Proteins 71(2);874-90. PMID: 18004749

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Cunningham98: Cunningham L, Guest JR (1998). "Transcription and transcript processing in the sdhCDAB-sucABCD operon of Escherichia coli." Microbiology 144 ( Pt 8);2113-23. PMID: 9720032

Darlison84: Darlison MG, Spencer ME, Guest JR (1984). "Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K-12." Eur J Biochem. 141(2):351-9. PMID: 6376123

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

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

Frank07: Frank RA, Price AJ, Northrop FD, Perham RN, Luisi BF (2007). "Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex." J Mol Biol 368(3);639-51. PMID: 17367808

Frank08: Frank RA, Kay CW, Hirst J, Luisi BF (2008). "Off-pathway, oxygen-dependent thiamine radical in the Krebs cycle." J Am Chem Soc 130(5);1662-8. PMID: 18183975

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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Gupta79a: Gupta SC, Dekker EE (1979). "Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli alpha-ketoglutarate dehydrogenase complex." Arch Biochem Biophys 192(1);324-6. PMID: 373631

Gupta80: Gupta SC, Dekker EE (1980). "Evidence for the identity and some comparative properties of alpha-ketoglutarate and 2-keto-4-hydroxyglutarate dehydrogenase activity." J Biol Chem 255(3);1107-12. PMID: 6985904

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

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

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Lindsay00: Lindsay H, Beaumont E, Richards SD, Kelly SM, Sanderson SJ, Price NC, Lindsay JG (2000). "FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli." J Biol Chem 275(47);36665-70. PMID: 10970889

Magnusson86: Magnusson K, Philips MK, Guest JR, Rutberg L (1986). "Nucleotide sequence of the gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex." J Bacteriol 1986;166(3);1067-71. PMID: 3086287

Murphy05: Murphy GE, Jensen GJ (2005). "Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes." Structure 13(12);1765-73. PMID: 16338405

Park97: Park SJ, Chao G, Gunsalus RP (1997). "Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter." J Bacteriol 179(13);4138-42. PMID: 9209026

Perham00: Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions." Annu Rev Biochem 69;961-1004. PMID: 10966480

Perham02: Perham RN, Jones DD, Chauhan HJ, Howard MJ (2002). "Substrate channelling in 2-oxo acid dehydrogenase multienzyme complexes." Biochem Soc Trans 30(2);47-51. PMID: 12023822

Perham87: Perham RN, Packman LC, Radford SE (1987). "2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning and halfway there." Biochem Soc Symp 1987;54;67-81. PMID: 3332999

Perham89: Perham RN, Packman LC (1989). "2-Oxo acid dehydrogenase multienzyme complexes: domains, dynamics, and design." Ann N Y Acad Sci 1989;573;1-20. PMID: 2699393

Pettit73: Pettit FH, Hamilton L, Munk P, Namihira G, Eley MH, Willms CR, Reed LJ (1973). "Alpha-keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex." J Biol Chem 248(15);5282-90. PMID: 4588679

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Reed01: Reed LJ (2001). "A trail of research from lipoic acid to alpha-keto acid dehydrogenase complexes." J Biol Chem 276(42);38329-36. PMID: 11477096

Reed74: Reed LJ "Multienzymes complexes." Accounts of Chemical Research 1974;7:40-46.

Shim11: Shim da J, Nemeria NS, Balakrishnan A, Patel H, Song J, Wang J, Jordan F, Farinas ET (2011). "Assignment of function to histidines 260 and 298 by engineering the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase complex; substitutions that lead to acceptance of substrates lacking the 5-carboxyl group." Biochemistry 50(35);7705-9. PMID: 21809826

Spencer82: Spencer ME, Guest JR (1982). "Molecular cloning of four tricarboxylic acid cyclic genes of Escherichia coli." J Bacteriol 151(2);542-52. PMID: 6284701

Spencer85: Spencer ME, Guest JR (1985). "Transcription analysis of the sucAB, aceEF and lpd genes of Escherichia coli." Mol Gen Genet 1985;200(1);145-54. PMID: 3897791

Steginsky85: Steginsky CA, Gruys KJ, Frey PA (1985). "alpha-Ketoglutarate dehydrogenase complex of Escherichia coli. A hybrid complex containing pyruvate dehydrogenase subunits from pyruvate dehydrogenase complex." J Biol Chem 260(25);13690-3. PMID: 3902822

Stephens83: Stephens PE, Darlison MG, Lewis HM, Guest JR (1983). "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component." Eur J Biochem 1983;133(3);481-9. PMID: 6345153

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

Waskiewicz84: Waskiewicz DE, Hammes GG (1984). "Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation." Biochemistry 23(14);3136-43. PMID: 6380583

Wood84: Wood D, Darlison MG, Wilde RJ, Guest JR (1984). "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli." Biochem J 1984;222(2);519-34. PMID: 6383359

Yu06: Yu BJ, Sung BH, Lee JY, Son SH, Kim MS, Kim SC (2006). "sucAB and sucCD are mutually essential genes in Escherichia coli." FEMS Microbiol Lett 254(2);245-50. PMID: 16445752

Other References Related to Gene Regulation

Desnoyers12: Desnoyers G, Masse E (2012). "Noncanonical repression of translation initiation through small RNA recruitment of the RNA chaperone Hfq." Genes Dev 26(7);726-39. PMID: 22474262

Geissmann04: Geissmann TA, Touati D (2004). "Hfq, a new chaperoning role: binding to messenger RNA determines access for small RNA regulator." EMBO J 23(2);396-405. PMID: 14739933

Iuchi88: Iuchi S, Lin EC (1988). "arcA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways." Proc Natl Acad Sci U S A 1988;85(6);1888-92. PMID: 2964639

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

Lynch96: Lynch AS, Lin EC (1996). "Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: characterization of DNA binding at target promoters." J Bacteriol 1996;178(21);6238-49. PMID: 8892825

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

Masse02: Masse E, Gottesman S (2002). "A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli." Proc Natl Acad Sci U S A 99(7);4620-5. PMID: 11917098

Park95a: Park SJ, Tseng CP, Gunsalus RP (1995). "Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: role of ArcA and Fnr." Mol Microbiol 15(3);473-82. PMID: 7783618

Salmon05: Salmon KA, Hung SP, Steffen NR, Krupp R, Baldi P, Hatfield GW, Gunsalus RP (2005). "Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA." J Biol Chem 280(15);15084-96. PMID: 15699038

Shen97: Shen J, Gunsalus RP (1997). "Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB) gene expression in Escherichia coli." Mol Microbiol 26(2);223-36. PMID: 9383149

Spiro91: Spiro S, Guest JR (1991). "Adaptive responses to oxygen limitation in Escherichia coli." Trends Biochem Sci 1991;16(8);310-4. PMID: 1957353

Trotter11: Trotter EW, Rolfe MD, Hounslow AM, Craven CJ, Williamson MP, Sanguinetti G, Poole RK, Green J (2011). "Reprogramming of Escherichia coli K-12 metabolism during the initial phase of transition from an anaerobic to a micro-aerobic environment." PLoS One 6(9);e25501. PMID: 21980479

Wilde86: Wilde RJ, Guest JR (1986). "Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12." J Gen Microbiol 1986;132 ( Pt 12);3239-51. PMID: 3309132

Wright13: Wright PR, Richter AS, Papenfort K, Mann M, Vogel J, Hess WR, Backofen R, Georg J (2013). "Comparative genomics boosts target prediction for bacterial small RNAs." Proc Natl Acad Sci U S A 110(37);E3487-96. PMID: 23980183

Zhang05: Zhang Z, Gosset G, Barabote R, Gonzalez CS, Cuevas WA, Saier MH (2005). "Functional interactions between the carbon and iron utilization regulators, Crp and Fur, in Escherichia coli." J Bacteriol 187(3);980-90. PMID: 15659676

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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