Escherichia coli K-12 substr. MG1655 Enzyme: isocitrate dehydrogenase phosphatase / isocitrate dehydrogenase kinase

Gene: aceK Accession Numbers: EG10026 (EcoCyc), b4016, ECK4008

Regulation Summary Diagram: ?

Regulation summary diagram for aceK

Subunit composition of isocitrate dehydrogenase phosphatase / isocitrate dehydrogenase kinase = [AceK]2

Isocitrate dehydrogenase kinase/phosphatase (AceK) controls a branch point between two pathways of central metabolism, the TCA cycle I (prokaryotic) and the glyoxylate cycle, shown in the superpathway of glyoxylate bypass and TCA. It controls the flux between the two cycles by controlling the activity of isocitrate dehydrogenase (IDH), an enzyme of the TCA cycle [Walsh84, LaPorte84, Walsh85a]. By phosphorylating and thus inactivating IDH [Borthwick84], its substrate isocitrate is diverted to the glyoxylate cycle enzyme, isocitrate lyase. By dephosphorylating and thus activating IDH, this enzyme's stronger affinity for isocitrate feeds it into the TCA cycle.

Phosphorylation and dephosphorylation of IDH were found to be carried out by the same enzyme, AceK [LaPorte82]. A conformational switch that is induced by AMP appears to determine whether AceK acts as a kinase or a phosphatase [Zheng10]. AceK also exhibits a high intrinsic ATPase activity [Stueland87, Rittinger96, Miller96]. Modelling of the mechanism for achieving robust levels of IDH activity suggests the existence of a ternary complex between AceK, non-phosphorylated IDH and phosphorylated IDH [Shinar09].

AceK acts on a serine residue at the active site of IDH [Thorsness87]; the enzyme recognizes only the intact IDH [McKee89a]. Regulators of the kinase/phosphatase activities act either via binding to the active site of the protein substrate IDH (such as NADPH and isocitrate) or via binding to the kinase/phosphatase itself (such as AMP, 3-phosphoglycerate and pyruvate) [Miller00a].

AceK has been crystallized both alone [Zheng09], in complex with isocitrate dehydrogenase [Zheng09a], and with AMP [Zheng10]. Except for the ATP binding motif, AceK lacks sequence homology with eukaryotic kinases and phosphatases; nevertheless, the structure of the C-terminal kinase domain of AceK is similar to eukaryotic protein kinases. In addition, an N-terminal regulatory domain with a novel fold was discovered, with AMP binding to an allosteric site between the kinase and the regulatory domain. The substrate recognition loop of AceK was found to be inserted deeply inside the active site cleft of IDH, enabling access to the otherwise buried active site Ser113 residue [Zheng10].

There appears to be only one ATP-binding site per subunit [Varela88, Rittinger96]. A mutation in the predicted ATP binding site leads to loss of both the kinase and phosphatase activities of the enzyme [Stueland89]. The phosphatase reaction does not proceed in the presence of a non-hydrolyzable ATP analog [Miller96]. Mutant alleles separating the kinase and phosphatase activities of the enzyme have been obtained [Ikeda91, Ikeda92]. A kinetic model for the mechanism of the kinase and phosphatase activities of the enzyme with a single active site has been proposed [Miller96]. Site-directed mutagenesis of the predicted "catalytic triad" residues found that only one, Asp371, is essential for activity, while Asn377 and Asp403 appear to be involved in Mg2+ binding [Oudot01]. Under non-reducing conditions, an intermolecular disulfide bond involving the C67 residue of both monomers is formed [Oudot99].

aceK expression is much lower than expression of the aceB and aceA genes upstream in the same operon [Cortay88]; this effect appears to be due to inefficient translation of aceK [Chung93]. aceK is essential for growth on acetate [elMansi87].

Reviews: [Laporte89, LaPorte93, Cozzone05]

Gene Citations: [Zaslaver06, Maloy82, LaPorte85]

Locations: cytosol

Map Position: [4,216,619 -> 4,218,355] (90.88 centisomes, 327°)
Length: 1737 bp / 578 aa

Molecular Weight of Polypeptide: 67.699 kD (from nucleotide sequence), 66.0 kD (experimental) [LaPorte82 ]

Molecular Weight of Multimer: 135.0 kD (experimental) [Nimmo84a]

Unification Links: ASAP:ABE-0013131 , CGSC:17770 , DIP:DIP-9041N , EchoBASE:EB0025 , EcoGene:EG10026 , EcoliWiki:b4016 , Mint:MINT-1711235 , OU-Microarray:b4016 , PortEco:aceK , PR:PRO_000022040 , Protein Model Portal:P11071 , RefSeq:NP_418440 , RegulonDB:EG10026 , SMR:P11071 , String:511145.b4016 , UniProt:P11071

Relationship Links: InterPro:IN-FAMILY:IPR010452 , PDB:Structure:3EPS , PDB:Structure:3IC6 , PDB:Structure:3ICB , Pfam:IN-FAMILY:PF06315 , ProDom:IN-FAMILY:PD043552

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for aceK

GO Terms:

Biological Process: GO:0016311 - dephosphorylation Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Miller96]
GO:0018105 - peptidyl-serine phosphorylation Inferred from experiment [Thorsness87]
GO:0050790 - regulation of catalytic activity Inferred from experiment [LaPorte82]
GO:0006006 - glucose metabolic process Inferred by computational analysis [GOA01a]
GO:0006097 - glyoxylate cycle Inferred by curator Inferred by computational analysis [UniProtGOA11a, GOA06, LaPorte82]
GO:0006099 - tricarboxylic acid cycle Inferred by curator Inferred by computational analysis [UniProtGOA11a, GOA06, LaPorte82]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0004674 - protein serine/threonine kinase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Thorsness87]
GO:0004722 - protein serine/threonine phosphatase activity Inferred from experiment [Miller96]
GO:0005524 - ATP binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, LaPorte82, Rittinger96]
GO:0008772 - [isocitrate dehydrogenase (NADP+)] kinase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, LaPorte82]
GO:0016208 - AMP binding Inferred from experiment [Zheng10]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0004721 - phosphoprotein phosphatase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016788 - hydrolase activity, acting on ester bonds Inferred by computational analysis [GOA06]
GO:0016791 - phosphatase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred by curator Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a, LaPorte82]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer protein related posttranslational modification
metabolism central intermediary metabolism glyoxylate bypass
regulation type of regulation posttranscriptional covalent modification, demodification, maturation

Essentiality data for aceK 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]

Last-Curated ? 18-Jun-2010 by Keseler I , SRI International

Enzymatic reaction of: isocitrate dehydrogenase phosphatase

Synonyms: ICDH phosphatase

EC Number: 3.1.3.-

a phosphorylated isocitrate dehydrogenase + H2O <=> an isocitrate dehydrogenase + phosphate

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 irreversible in the direction shown.

The phosphatase reaction requires the presence of either ATP or ADP [LaPorte82]. The Km for ATP in the phosphatase reaction is 6 µM [Miller96]. Isocitrate "activates" the phosphatase activity by binding to the active site of dephospho-IDH and thereby preventing product inhibition [Miller00a].

Cofactors or Prosthetic Groups: Mg2+ [Nimmo84]

Activators (Unknown Mechanism): isocitrate [Nimmo84] , ATP [Nimmo84a] , 2-oxoglutarate [Nimmo84] , oxaloacetate [Nimmo84] , ADP [Nimmo84a] , AMP [Nimmo84, Miller00a] , phosphoenolpyruvate [Nimmo84] , 3-phospho-D-glycerate [Miller00a] , pyruvate [Nimmo84, Miller00a, Comment 4]

Inhibitors (Competitive): NADPH [Nimmo84, Miller00a]

Kinetic Parameters:

Km (μM)
a phosphorylated isocitrate dehydrogenase

pH(opt): 6.1-6.7 [Nimmo84]

Enzymatic reaction of: isocitrate dehydrogenase kinase

Synonyms: ICDH kinase

EC Number:

an isocitrate dehydrogenase + ATP <=> ADP + a phosphorylated isocitrate dehydrogenase

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 irreversible in the direction shown.

Cofactors or Prosthetic Groups: Mg2+ [Oudot01, Nimmo84a]

Inhibitors (Competitive): isocitrate [Nimmo84, Miller00a] , NADPH [Nimmo84, Miller00a]

Inhibitors (Unknown Mechanism): ADP [Nimmo84] , AMP [Nimmo84, Miller00a] , oxaloacetate [Nimmo84] , 2-oxoglutarate [Nimmo84] , phosphoenolpyruvate [Nimmo84] , 3-phospho-D-glycerate [Miller00a] , pyruvate [Nimmo84, Miller00a] , NADP+ [Nimmo84] , citrate [Nimmo84] , β-D-fructofuranose 6-phosphate [Nimmo84] , glyoxylate [Nimmo84]

Kinetic Parameters:

Km (μM)
an isocitrate dehydrogenase

pH(opt): 8-8.5 [Nimmo84]

Sequence Features

Protein sequence of AceK with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
Sequence-Conflict 140
[Cortay88, UniProt10]
UniProt: (in Ref. 2; AAA24007);
Nucleotide-Phosphate-Binding-Region 315 -> 321
UniProt: ATP; Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 336
[Laporte89, UniProt11]
UniProt: Inhibits enzyme.
Amino-Acid-Sites-That-Bind 336
UniProt: ATP; Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 371
[Oudot01, UniProt11]
D → A, E or Q: Loss of activity.
Active-Site 371
UniProt: Non-Experimental Qualifier: probable;
Mutagenesis-Variant 377
[Oudot01, UniProt11]
UniProt: No loss of activity.
Mutagenesis-Variant 403
[Oudot01, UniProt11]
UniProt: No loss of activity.
Sequence-Conflict 416 -> 417
[Klumpp88, UniProt10]
UniProt: (in Ref. 1; AAA24010);
Mutagenesis-Variant 439
[Oudot01, UniProt11]
UniProt: No loss of activity.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b4016 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10026; 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

Borthwick84: Borthwick AC, Holms WH, Nimmo HG (1984). "The phosphorylation of Escherichia coli isocitrate dehydrogenase in intact cells." Biochem J 1984;222(3);797-804. PMID: 6385963

Chung93: Chung T, Resnik E, Stueland C, LaPorte DC (1993). "Relative expression of the products of glyoxylate bypass operon: contributions of transcription and translation." J Bacteriol 175(14);4572-5. PMID: 8331088

Cortay88: Cortay JC, Bleicher F, Rieul C, Reeves HC, Cozzone AJ (1988). "Nucleotide sequence and expression of the aceK gene coding for isocitrate dehydrogenase kinase/phosphatase in Escherichia coli." J Bacteriol 1988;170(1);89-97. PMID: 2826408

Cozzone05: Cozzone AJ, El-Mansi M (2005). "Control of isocitrate dehydrogenase catalytic activity by protein phosphorylation in Escherichia coli." J Mol Microbiol Biotechnol 9(3-4);132-46. PMID: 16415587

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

elMansi87: el-Mansi EM, MacKintosh C, Duncan K, Holms WH, Nimmo HG (1987). "Molecular cloning and over-expression of the glyoxylate bypass operon from Escherichia coli ML308." Biochem J 242(3);661-5. PMID: 3297049

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."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Ikeda91: Ikeda T, LaPorte DC (1991). "Isocitrate dehydrogenase kinase/phosphatase: aceK alleles that express kinase but not phosphatase activity." J Bacteriol 173(5);1801-6. PMID: 1847910

Ikeda92: Ikeda TP, Houtz E, LaPorte DC (1992). "Isocitrate dehydrogenase kinase/phosphatase: identification of mutations which selectively inhibit phosphatase activity." J Bacteriol 174(4);1414-6. PMID: 1310504

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

Klumpp88: Klumpp DJ, Plank DW, Bowdin LJ, Stueland CS, Chung T, LaPorte DC (1988). "Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase." J Bacteriol 170(6);2763-9. PMID: 2836370

LaPorte82: LaPorte DC, Koshland DE (1982). "A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle." Nature 1982;300(5891);458-60. PMID: 6292732

LaPorte84: LaPorte DC, Walsh K, Koshland DE (1984). "The branch point effect. Ultrasensitivity and subsensitivity to metabolic control." J Biol Chem 1984;259(22);14068-75. PMID: 6389540

LaPorte85: LaPorte DC, Thorsness PE, Koshland DE (1985). "Compensatory phosphorylation of isocitrate dehydrogenase. A mechanism for adaptation to the intracellular environment." J Biol Chem 260(19);10563-8. PMID: 3897222

Laporte89: Laporte DC, Stueland CS, Ikeda TP (1989). "Isocitrate dehydrogenase kinase/phosphatase." Biochimie 71(9-10);1051-7. PMID: 2557093

LaPorte93: LaPorte DC (1993). "The isocitrate dehydrogenase phosphorylation cycle: regulation and enzymology." J Cell Biochem 51(1);14-8. PMID: 8381789

Maloy82: Maloy SR, Nunn WD (1982). "Genetic regulation of the glyoxylate shunt in Escherichia coli K-12." J Bacteriol 1982;149(1);173-80. PMID: 7033207

McKee89a: McKee JS, Hlodan R, Nimmo HG (1989). "Studies of the phosphorylation of Escherichia coli isocitrate dehydrogenase. Recognition of the enzyme by isocitrate dehydrogenase kinase/phosphatase and effects of phosphorylation on its structure and properties." Biochimie 71(9-10);1059-64. PMID: 2557094

Miller00a: Miller SP, Chen R, Karschnia EJ, Romfo C, Dean A, LaPorte DC (2000). "Locations of the regulatory sites for isocitrate dehydrogenase kinase/phosphatase." J Biol Chem 275(2);833-9. PMID: 10625615

Miller96: Miller SP, Karschnia EJ, Ikeda TP, LaPorte DC (1996). "Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins." J Biol Chem 271(32);19124-8. PMID: 8702587

Nimmo84: Nimmo GA, Nimmo HG (1984). "The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli ML308 and the roles of these activities in the control of isocitrate dehydrogenase." Eur J Biochem 1984;141(2);409-14. PMID: 6329757

Nimmo84a: Nimmo GA, Borthwick AC, Holms WH, Nimmo HG (1984). "Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308." Eur J Biochem 141(2);401-8. PMID: 6329756

Oudot01: Oudot C, Cortay JC, Blanchet C, Laporte DC, Di Pietro A, Cozzone AJ, Jault JM (2001). "The "catalytic" triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases." Biochemistry 40(10);3047-55. PMID: 11258918

Oudot99: Oudot C, Jaquinod M, Cortay JC, Cozzone AJ, Jault JM (1999). "The isocitrate dehydrogenase kinase/phosphatase from Escherichia coli is highly sensitive to in-vitro oxidative conditions role of cysteine67 and cysteine108 in the formation of a disulfide-bonded homodimer." Eur J Biochem 1999;262(1);224-9. PMID: 10231385

Rittinger96: Rittinger K, Negre D, Divita G, Scarabel M, Bonod-Bidaud C, Goody RS, Cozzone AJ, Cortay JC (1996). "Escherichia coli isocitrate dehydrogenase kinase/phosphatase. Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues." Eur J Biochem 237(1);247-54. PMID: 8620880

Shinar09: Shinar G, Rabinowitz JD, Alon U (2009). "Robustness in glyoxylate bypass regulation." PLoS Comput Biol 5(3);e1000297. PMID: 19266029

Stueland87: Stueland CS, Eck KR, Stieglbauer KT, LaPorte DC (1987). "Isocitrate dehydrogenase kinase/phosphatase exhibits an intrinsic adenosine triphosphatase activity." J Biol Chem 262(33);16095-9. PMID: 2824478

Stueland89: Stueland CS, Ikeda TP, LaPorte DC (1989). "Mutation of the predicted ATP binding site inactivates both activities of isocitrate dehydrogenase kinase/phosphatase." J Biol Chem 264(23);13775-9. PMID: 2547774

Thorsness87: Thorsness PE, Koshland DE (1987). "Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate." J Biol Chem 1987;262(22);10422-5. PMID: 3112144

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: 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 the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

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

Varela88: Varela I, Nimmo HG (1988). "Photoaffinity labelling shows that Escherichia coli isocitrate dehydrogenase kinase/phosphatase contains a single ATP-binding site." FEBS Lett 231(2);361-5. PMID: 2834232

Walsh84: Walsh K, Koshland DE (1984). "Determination of flux through the branch point of two metabolic cycles. The tricarboxylic acid cycle and the glyoxylate shunt." J Biol Chem 1984;259(15);9646-54. PMID: 6378912

Walsh85a: Walsh K, Koshland DE (1985). "Branch point control by the phosphorylation state of isocitrate dehydrogenase. A quantitative examination of fluxes during a regulatory transition." J Biol Chem 1985;260(14);8430-7. PMID: 2861202

Zaslaver06: Zaslaver A, Bren A, Ronen M, Itzkovitz S, Kikoin I, Shavit S, Liebermeister W, Surette MG, Alon U (2006). "A comprehensive library of fluorescent transcriptional reporters for Escherichia coli." Nat Methods 3(8);623-8. PMID: 16862137

Zheng09: Zheng J, Lee DC, Jia Z (2009). "Purification, crystallization and preliminary X-ray analysis of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli." Acta Crystallogr Sect F Struct Biol Cryst Commun 65(Pt 5);536-9. PMID: 19407397

Zheng09a: Zheng J, Ji AX, Jia Z (2009). "Purification, crystallization and preliminary X-ray analysis of bifunctional isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli." Acta Crystallogr Sect F Struct Biol Cryst Commun 65(Pt 11);1153-6. PMID: 19923739

Zheng10: Zheng J, Jia Z (2010). "Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase." Nature 465(7300);961-5. PMID: 20505668

Other References Related to Gene Regulation

Chin89: Chin AM, Feldheim DA, Saier MH (1989). "Altered transcriptional patterns affecting several metabolic pathways in strains of Salmonella typhimurium which overexpress the fructose regulon." J Bacteriol 171(5);2424-34. PMID: 2496106

Cortay91: Cortay JC, Negre D, Galinier A, Duclos B, Perriere G, Cozzone AJ (1991). "Regulation of the acetate operon in Escherichia coli: purification and functional characterization of the IclR repressor." EMBO J 1991;10(3);675-9. PMID: 2001680

Cortay94: Cortay JC, Negre D, Scarabel M, Ramseier TM, Vartak NB, Reizer J, Saier MH, Cozzone AJ (1994). "In vitro asymmetric binding of the pleiotropic regulatory protein, FruR, to the ace operator controlling glyoxylate shunt enzyme synthesis." J Biol Chem 1994;269(21);14885-91. PMID: 8195118

Donald01: Donald LJ, Hosfield DJ, Cuvelier SL, Ens W, Standing KG, Duckworth HW (2001). "Mass spectrometric study of the Escherichia coli repressor proteins, Ic1R and Gc1R, and their complexes with DNA." Protein Sci 10(7);1370-80. PMID: 11420439

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

Lorca07: Lorca GL, Ezersky A, Lunin VV, Walker JR, Altamentova S, Evdokimova E, Vedadi M, Bochkarev A, Savchenko A (2007). "Glyoxylate and pyruvate are antagonistic effectors of the Escherichia coli IclR transcriptional regulator." J Biol Chem 282(22);16476-91. PMID: 17426033

Negre92: Negre D, Cortay JC, Galinier A, Sauve P, Cozzone AJ (1992). "Specific interactions between the IclR repressor of the acetate operon of Escherichia coli and its operator." J Mol Biol 1992;228(1);23-9. PMID: 1447784

Pan96: Pan B, Unnikrishnan I, LaPorte DC (1996). "The binding site of the IclR repressor protein overlaps the promoter of aceBAK." J Bacteriol 178(13);3982-4. PMID: 8682810

Ramseier93: Ramseier TM, Negre D, Cortay JC, Scarabel M, Cozzone AJ, Saier MH (1993). "In vitro binding of the pleiotropic transcriptional regulatory protein, FruR, to the fru, pps, ace, pts and icd operons of Escherichia coli and Salmonella typhimurium." J Mol Biol 234(1);28-44. PMID: 8230205

Resnik96: Resnik E, Pan B, Ramani N, Freundlich M, LaPorte DC (1996). "Integration host factor amplifies the induction of the aceBAK operon of Escherichia coli by relieving IclR repression." J Bacteriol 1996;178(9);2715-7. PMID: 8626344

Son11: Son YJ, Phue JN, Trinh LB, Lee SJ, Shiloach J (2011). "The role of Cra in regulating acetate excretion and osmotic tolerance in E. coli K-12 and E. coli B at high density growth." Microb Cell Fact 10;52. PMID: 21718532

Waegeman11: Waegeman H, Beauprez J, Moens H, Maertens J, De Mey M, Foulquie-Moreno MR, Heijnen JJ, Charlier D, Soetaert W (2011). "Effect of iclR and arcA knockouts on biomass formation and metabolic fluxes in Escherichia coli K12 and its implications on understanding the metabolism of Escherichia coli BL21 (DE3)." BMC Microbiol 11;70. PMID: 21481254

Yamamoto03: Yamamoto K, Ishihama A (2003). "Two different modes of transcription repression of the Escherichia coli acetate operon by IclR." Mol Microbiol 47(1);183-94. PMID: 12492863

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

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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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