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Escherichia coli K-12 substr. MG1655 Enzyme: dihydrolipoyltranssuccinylase



Gene: sucB Accession Numbers: EG10980 (EcoCyc), b0727, ECK0715

Synonyms: E2(o) subunit

Regulation Summary Diagram: ?

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

Subunit composition of dihydrolipoyltranssuccinylase = [SucB]24

Alternative forms of SucB:
SucB-dihydrolipoate
SucB-S-succinyldihydrolipoate
SucB-lipoate

Summary:
E. coli SucB is responsible for the dihydrolipoyltranssuccinylase (dihydrolipoamide succinyltransferase) activity of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDHC) that catalyzes the conversion of 2-oxoglutarate (2-ketoglutarate) to succinyl-CoA and carbon dioxide, with the production of NADH (see 2-oxoglutarate decarboxylation to succinyl-CoA). SucB catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A, forming 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) component 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].

SucB has a single lipoyl domain at the N-terminus, and a domain with catalytic and subunit binding activity at the C-terminus. It also has areas that contain a large amount of alanine and proline [Spencer84]. The domain structure has been examined by limited proteolysis experiments [Packman87]. Data has suggested that E2(o) has a role in substrate specificity and channeling [Shim11, Perham02]. SucB is lipoylated by LipB, or LplA [Hassan11] (see the reactions below).

The crystal structure of the catalytic domain of SucB provided insights into its interaction with the lipoyl domain [Knapp00, Knapp98]. The crystal structure of the lipoyl domain has also been determined [Ricaud96]. This domain has also been studied by analysis of NMR spectra [Robien92, Ferguson05, Neuweiler09, Jones08].

SucB (E2(o)) has similarity to the AceF (E2(p)) subunit of the pyruvate dehydrogenase multienzyme complex although the N-terminal domain of AceF contains three lipoyl repeats, whereas SucB contains only one of these sequences [Spencer84]. E. coli SucB has similarity to Coxiella burnetii SucB, which elicits an immune response in infected humans [Nguyen99]. The Mycobacterium tuberculosis SucB is involved in a protective antioxidant response to attack by the immune system [Bryk02].

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 sucB gene was cloned and sequenced in earlier work [Spencer82, Spencer84] and the initial sequence of the gene was corrected [Packman87]. Transcription of the sucB gene has been analyzed in relation to other members of its gene cluster [Spencer85, Buck85, Buck86, 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 [Yu06a]. SucB and SucC were induced during growth at low pH [Stancik02]. Mutant studies showed that the sucB gene is involved in resistance to antibiotics and other stresses in a persister population of E. coli [Ma10].

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

Gene Citations: [Wood84, Magnusson86, Buck89]

Locations: cytosol

Map Position: [760,745 -> 761,962] (16.4 centisomes)
Length: 1218 bp / 405 aa

Molecular Weight of Polypeptide: 44.011 kD (from nucleotide sequence)

pI: 5.85

Unification Links: ASAP:ABE-0002480 , CGSC:145 , DIP:DIP-35787N , EchoBASE:EB0973 , EcoGene:EG10980 , EcoliWiki:b0727 , Mint:MINT-1242608 , OU-Microarray:b0727 , PortEco:sucB , PR:PRO_000024003 , Pride:P0AFG6 , Protein Model Portal:P0AFG6 , RegulonDB:EG10980 , SMR:P0AFG6 , String:511145.b0727 , Swiss-Model:P0AFG6 , UniProt:P0AFG6

Relationship Links: InterPro:IN-FAMILY:IPR000089 , InterPro:IN-FAMILY:IPR001078 , InterPro:IN-FAMILY:IPR003016 , InterPro:IN-FAMILY:IPR004167 , InterPro:IN-FAMILY:IPR006255 , InterPro:IN-FAMILY:IPR011053 , InterPro:IN-FAMILY:IPR023213 , PDB:Structure:1BAL , PDB:Structure:1BBL , PDB:Structure:1C4T , PDB:Structure:1E2O , PDB:Structure:1PMR , PDB:Structure:1SCZ , PDB:Structure:1W4H , PDB:Structure:2BTG , PDB:Structure:2BTH , PDB:Structure:2WXC , Pfam:IN-FAMILY:PF00198 , Pfam:IN-FAMILY:PF00364 , Pfam:IN-FAMILY:PF02817 , Prosite:IN-FAMILY:PS00189 , Prosite:IN-FAMILY:PS50968

In Paralogous Gene Group: 39 (2 members)

In Reactions of unknown directionality:

Not in pathways:
ATP + SucB + (R)-lipoate = AMP + SucB-lipoate + diphosphate
SucB + lipoyl-ACP = SucB-lipoate + a holo-[acyl-carrier protein]

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006099 - tricarboxylic acid cycle Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Spencer82]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0033512 - L-lysine catabolic process to acetyl-CoA via saccharopine Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0004149 - dihydrolipoyllysine-residue succinyltransferase activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Spencer82, Willms67]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05]
GO:0031405 - lipoic acid binding Inferred from experiment [Packman91]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016746 - transferase activity, transferring acyl groups Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Molloy00, LopezCampistrou05]
GO:0045252 - oxoglutarate dehydrogenase complex Inferred from experiment Inferred by computational analysis [GOA01, Willms67]

MultiFun Terms: metabolism energy metabolism, carbon TCA cycle

Essentiality data for sucB 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]

Credits:
Last-Curated ? 22-Jun-2012 by Fulcher C , SRI International


Enzymatic reaction of: dihydrolipoyltranssuccinylase

Synonyms: lipoate succinyltransferase, dihydrolipoamide succinyltransferase, lipoamide acyltransferase

EC Number: 2.3.1.61

succinyl-CoA + a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine <=> a [2-oxoglutarate dehydrogenase E2 protein] N6-S-succinyldihydrolipoyl-L-lysine + coenzyme A

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


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

Summary:
The 2-oxoglutarate (2-ketoglutarate) dehydrogenase complex is similar in enzyme composition and complex reactions to the pyruvate dehydrogenase complex reactions [Perham87, Stephens83a, 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)

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

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


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Link97, UniProt11a]
UniProt: Removed.
Conserved-Region 2 -> 77
[UniProt09]
UniProt: Lipoyl-binding;
Chain 2 -> 405
[UniProt09]
UniProt: Dihydrolipoyllysine-residue succinyltransferase component of 2- oxoglutarate dehydrogenase complex;
N6-lipoyllysine-Modification 44
[UniProt11]
UniProt: N6-lipoyllysine.
Acetylation-Modification 148
[Zhang09, UniProt11a]
UniProt: N6-acetyllysine.
Acetylation-Modification 226
[Yu08]
 
Active-Site 376
[UniProt10]
Active-Site 380
[UniProt10]


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0727 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10980; confirmed by SwissProt match.


References

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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

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Ferguson05: Ferguson N, Sharpe TD, Schartau PJ, Sato S, Allen MD, Johnson CM, Rutherford TJ, Fersht AR (2005). "Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family." J Mol Biol 353(2);427-46. PMID: 16168437

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

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.

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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

Jones08: Jones DD, Perham RN (2008). "The role of loop and beta-turn residues as structural and functional determinants for the lipoyl domain from the Escherichia coli 2-oxoglutarate dehydrogenase complex." Biochem J 409(2);357-66. PMID: 17927566

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

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Knapp98: Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML (1998). "Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex." J Mol Biol 280(4);655-68. PMID: 9677295

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

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

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Ma10: Ma C, Sim S, Shi W, Du L, Xing D, Zhang Y (2010). "Energy production genes sucB and ubiF are involved in persister survival and tolerance to multiple antibiotics and stresses in Escherichia coli." FEMS Microbiol Lett 303(1);33-40. PMID: 20041955

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

Molloy00: Molloy MP, Herbert BR, Slade MB, Rabilloud T, Nouwens AS, Williams KL, Gooley AA (2000). "Proteomic analysis of the Escherichia coli outer membrane." Eur J Biochem 267(10);2871-81. PMID: 10806384

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

Neuweiler09: Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR (2009). "The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family." J Mol Biol 390(5);1060-73. PMID: 19445954

Nguyen99: Nguyen SV, To H, Yamaguchi T, Fukushi H, Hirai K (1999). "Characterization of the Coxiella burnetti sucB gene encoding an immunogenic dihydrolipoamide succinyltransferase." Microbiol Immunol 43(8);743-9. PMID: 10524791

Packman87: Packman LC, Perham RN (1987). "Limited proteolysis and sequence analysis of the 2-oxo acid dehydrogenase complexes from Escherichia coli. Cleavage sites and domains in the dihydrolipoamide acyltransferase components." Biochem J 242(2);531-8. PMID: 3297046

Packman91: Packman LC, Green B, Perham RN (1991). "Lipoylation of the E2 components of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli." Biochem J 277 ( Pt 1);153-8. PMID: 1854331

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.

Ricaud96: Ricaud PM, Howard MJ, Roberts EL, Broadhurst RW, Perham RN (1996). "Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli." J Mol Biol 264(1);179-90. PMID: 8950276

Robien92: Robien MA, Clore GM, Omichinski JG, Perham RN, Appella E, Sakaguchi K, Gronenborn AM (1992). "Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli." Biochemistry 31(13);3463-71. PMID: 1554728

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

Spencer84: Spencer ME, Darlison MG, Stephens PE, Duckenfield IK, Guest JR (1984). "Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase." Eur J Biochem 141(2);361-74. PMID: 6376124

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

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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

Stephens83a: 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

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

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

UniProt11: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

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

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

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

Willms67: Willms CR, Oliver RM, Henney HR, Mukherjee BB, Reed LJ (1967). "Alpha-keto acid dehydrogenase complexes. VI. Dissociation and reconstitution of the dihydrolipoyl transacetylase of Escherichia coli." J Biol Chem 242(5);889-97. PMID: 5335914

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

Yu06a: 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

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

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

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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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