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Escherichia coli K-12 substr. MG1655 Enzyme: phosphoenolpyruvate carboxykinase (ATP)



Gene: pck Accession Numbers: EG10688 (EcoCyc), b3403, ECK3390

Synonyms: pckA

Regulation Summary Diagram: ?

Summary:
Phosphoenolpyruvate (PEP) carboxykinase (Pck) is an enzyme involved in gluconeogenesis. Growth on succinate as the carbon and energy sourse is limited by the level of Pck in the cell [Chao93].

PEP carboxykinase is unusual in that it appears to be a monomeric enzyme with an allosteric site [Goldie80a].

Crystal structures of the enzyme have been solved [Delbaere91, Matte96, Tari96, Sudom01, Sudom03], providing insight into the mechanistic details of the enzymatic reaction [Tari96, Sudom01] and into the mechanism of activation by Ca2+ [Sudom03].

Transcription of pck is regulated by catabolite repression and is induced at the onset of stationary phase [Goldie80, Goldie84, Goldie90] and is regulated by CsrA [Romeo93]. Overexpression of pck during growth on glucose leads to reduced growth yield and increased excretion of fermentation products such as acetate [Chao93a]. Expression of Pck is upregulated when acetate is used as the source of carbon [Peng03].

A double mutant defective in both PEP carboxykinase and phosphoenolpyruvate synthetase is unable to utilize C4-dicarboxylic acids such as succinate and malate as the sole source of carbon and energy [Hansen74].

Reviews: [Liao94, Pai96, Matte97, Delbaere04]

Citations: [Goldie81, Medina90, Bazaes93, Bazaes95, Hou95, Encinas95, Bustos96, Bazaes97, Tari97, Encinas98, Lee99a, Encinas02]

Gene Citations: [Sabnis95, Oh00]

Locations: cytosol

Map Position: [3,530,840 -> 3,532,462] (76.1 centisomes)
Length: 1623 bp / 540 aa

Molecular Weight of Polypeptide: 59.643 kD (from nucleotide sequence), 55.0 kD (experimental) [Goldie90 ]

pI: 8.35

Unification Links: ASAP:ABE-0011106 , CGSC:422 , EchoBASE:EB0682 , EcoGene:EG10688 , EcoliWiki:b3403 , EcoO157Cyc:PCKA , ModBase:P22259 , OU-Microarray:b3403 , PortEco:pck , PR:PRO_000023498 , Pride:P22259 , Protein Model Portal:P22259 , RefSeq:NP_417862 , RegulonDB:EG10688 , SMR:P22259 , String:511145.b3403 , UniProt:P22259

Relationship Links: InterPro:IN-FAMILY:IPR001272 , InterPro:IN-FAMILY:IPR008210 , InterPro:IN-FAMILY:IPR013035 , InterPro:IN-FAMILY:IPR015994 , PDB:Structure:1AQ2 , PDB:Structure:1AYL , PDB:Structure:1K3C , PDB:Structure:1K3D , PDB:Structure:1OEN , PDB:Structure:1OS1 , PDB:Structure:2OLQ , PDB:Structure:2OLR , PDB:Structure:2PXZ , PDB:Structure:2PY7 , Pfam:IN-FAMILY:PF01293 , Prosite:IN-FAMILY:PS00532

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006094 - gluconeogenesis Inferred from experiment Author statement Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06, GOA01a, Goldie80a, Hansen74]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment [Encinas93]
GO:0004612 - phosphoenolpyruvate carboxykinase (ATP) activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Goldie80a]
GO:0005509 - calcium ion binding Inferred from experiment [Sudom03]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a]
GO:0004611 - phosphoenolpyruvate carboxykinase activity Inferred by computational analysis [GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016831 - carboxy-lyase activity Inferred by computational analysis [UniProtGOA11a]
GO:0017076 - purine nucleotide binding Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism central intermediary metabolism

Essentiality data for pck 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]

Enzymatic reaction of: phosphoenolpyruvate carboxykinase (ATP)

Synonyms: phosphopyruvate carboxylase (ATP), phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxykinase, ATP:oxaloacetate carboxy-lyase (transphosphorylating)

EC Number: 4.1.1.49

oxaloacetate + ATP <=> CO2 + phosphoenolpyruvate + ADP

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: gluconeogenesis I

Summary:
Although early studies reported inhibition of the enzyme by NADH [Wright69, Krebs76], this was found to be due to contamination of the partially purified enzyme preparation by malate dehydrogenase and interference with the colorimetric assay reaction [Goldie80a].

The enyzme was initially purified from E. coli B [Wright69, Krebs76, Krebs80].

Cofactors or Prosthetic Groups: Mg2+ [Goldie80a]

Alternative Cofactors for Mg2+: Ca2+ , Mn2+

Activators (Unknown Mechanism): Ca2+ [Goldie80a, Sudom03]

Inhibitors (Unknown Mechanism): ATP [Krebs80] , phosphoenolpyruvate [Krebs80]

Kinetic Parameters:

Substrate
Km (μM)
Citations
oxaloacetate
670.0
[Krebs80, BRENDA14]
phosphoenolpyruvate
70.0
[Krebs80, BRENDA14]
phosphoenolpyruvate
500.0, 8000.0
[Krebs76, BRENDA14]
ADP
50.0
[Krebs80, BRENDA14]
ATP
60.0
[Krebs80, BRENDA14]


Sequence Features

Feature Class Location Attached Group Citations Comment
Mutagenesis-Variant 65  
[Cotelesage07, UniProt14]
Alternate sequence: R → Q; UniProt: Slightly lower catalytic efficiency compared to wild-type and the affinity binding for OAA is 330-fold higher than for wild-type.
Amino-Acid-Sites-That-Bind 65  
[UniProt14]
UniProt: Substrate.
Sequence-Conflict 67 -> 72  
[Medina90, UniProt10a]
Alternate sequence: PKDKYI → QKISIS; UniProt: (in Ref. 1; AAA24301);
Acetylation-Modification 87  
[Zhang09a, UniProt11]
UniProt: N6-acetyllysine.
Metal-Binding-Site 149  
[UniProt14]
UniProt: Calcium; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 150  
[UniProt14]
UniProt: Calcium; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 152  
[UniProt14]
UniProt: Calcium; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Sequence-Conflict 192 -> 194  
[Medina90, UniProt10a]
Alternate sequence: AFN → R; UniProt: (in Ref. 1; AA sequence);
Sequence-Conflict 197 -> 203  
[Medina90, UniProt10a]
Alternate sequence: ERMQLIG → DRAHAADC; UniProt: (in Ref. 1; AA sequence);
Amino-Acid-Sites-That-Bind 207  
[UniProt14]
UniProt: Substrate.
Metal-Binding-Site 213  
[UniProt14]
UniProt: Manganese.
Metal-Binding-Site 232  
[UniProt14]
UniProt: Manganese; via tele nitrogen.
Sequence-Conflict 233  
[Medina90, UniProt10a]
Alternate sequence: C → S; UniProt: (in Ref. 1; AAA24301);
Nucleotide-Phosphate-Binding-Region 248 -> 256 ATP
[UniProt14]
UniProt: ATP.
Sequence-Conflict 252  
[Medina90, UniProt10a]
Alternate sequence: T → N; UniProt: (in Ref. 1; AAA24301);
Sequence-Conflict 256 -> 260  
[Medina90, UniProt10a]
Alternate sequence: TLSTD → AFPR; UniProt: (in Ref. 1; AAA24301);
Mutagenesis-Variant 268  
[Hou95, UniProt11]
Alternate sequence: D → N; UniProt: In PCK51; altered-activity mutant that catalyzes the conversion from oxaloacetate to pyruvate (OAA decarboxylase activity).
Metal-Binding-Site 269  
[UniProt14]
UniProt: Manganese.
Sequence-Conflict 281 -> 285  
[Medina90, UniProt10a]
Alternate sequence: FEGGC → LKAAG; UniProt: (in Ref. 1; AAA24301);
Metal-Binding-Site 283  
[UniProt14]
UniProt: Calcium; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 284  
[Hou95, UniProt11]
Alternate sequence: G → S; UniProt: In PCK53; shows reduced-activity.
Amino-Acid-Sites-That-Bind 297  
[UniProt14]
UniProt: ATP.
Sequence-Conflict 302 -> 307  
[Medina90, UniProt10a]
Alternate sequence: NAIRRD → KLSVVM; UniProt: (in Ref. 1; AAA24301);
Amino-Acid-Sites-That-Bind 333  
[UniProt14]
UniProt: ATP.
Sequence-Conflict 346  
[Medina90, UniProt10a]
Alternate sequence: K → R; UniProt: (in Ref. 1; AAA24301);
Sequence-Conflict 354 -> 359  
[Medina90, UniProt10a]
Alternate sequence: ATKVIF → GRRLSL; UniProt: (in Ref. 1; AAA24301);
Sequence-Conflict 363  
[Medina90, UniProt10a]
Alternate sequence: D → H; UniProt: (in Ref. 1; AAA24301);
Sequence-Conflict 446  
[Medina90, UniProt10a]
Alternate sequence: T → S; UniProt: (in Ref. 1; AAA24301);
Nucleotide-Phosphate-Binding-Region 449 -> 450 ATP
[UniProt14]
UniProt: ATP.
Sequence-Conflict 449  
[Medina90, UniProt10a]
Alternate sequence: R → S; UniProt: (in Ref. 1; AAA24301);
Amino-Acid-Sites-That-Bind 455  
[UniProt14]
UniProt: ATP.
Sequence-Conflict 460 -> 467  
[Mizuno82, UniProt10a]
Alternate sequence: DAILNGSL → RRHPQRFV; UniProt: (in Ref. 4);
Sequence-Conflict 499  
[Mizuno82, UniProt10a]
Alternate sequence: T → R; UniProt: (in Ref. 4);
Acetylation-Modification 523  
[Zhang09a, UniProt11]
UniProt: N6-acetyllysine.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b3403 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10688; confirmed by SwissProt match.


References

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

Bazaes93: Bazaes S, Silva R, Goldie H, Cardemil E, Jabalquinto AM (1993). "Reactivity of cysteinyl, arginyl, and lysyl residues of Escherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents." J Protein Chem 12(5);571-7. PMID: 8141999

Bazaes95: Bazaes S, Goldie H, Cardemil E, Jabalquinto AM (1995). "Identification of reactive lysines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae." FEBS Lett 360(2);207-10. PMID: 7875332

Bazaes97: Bazaes S, Montecinos L, Krautwurst H, Goldie H, Cardemil E, Jabalquinto AM (1997). "Identification of reactive conserved histidines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae." Biochim Biophys Acta 1337(2);166-74. PMID: 9048893

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

Bustos96: Bustos P, Gajardo MI, Gomez C, Goldie H, Cardemil E, Jabalquinto AM (1996). "Woodward's reagent K reacts with histidine and cysteine residues in Escherichia coli and Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases." J Protein Chem 15(5);467-72. PMID: 8895092

Chao93: Chao YP, Patnaik R, Roof WD, Young RF, Liao JC (1993). "Control of gluconeogenic growth by pps and pck in Escherichia coli." J Bacteriol 175(21);6939-44. PMID: 8226637

Chao93a: Chao YP, Liao JC (1993). "Alteration of growth yield by overexpression of phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxykinase in Escherichia coli." Appl Environ Microbiol 59(12);4261-5. PMID: 8285716

Cotelesage07: Cotelesage JJ, Puttick J, Goldie H, Rajabi B, Novakovski B, Delbaere LT (2007). "How does an enzyme recognize CO2?." Int J Biochem Cell Biol 39(6);1204-10. PMID: 17475535

Delbaere04: Delbaere LT, Sudom AM, Prasad L, Leduc Y, Goldie H (2004). "Structure/function studies of phosphoryl transfer by phosphoenolpyruvate carboxykinase." Biochim Biophys Acta 1697(1-2);271-8. PMID: 15023367

Delbaere91: Delbaere LT, Vandonselaar M, Glaeske D, Jabs C, Goldie H (1991). "Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12." J Mol Biol 219(4);593-4. PMID: 2056527

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

Encinas02: Encinas MV, Gonzalez-Nilo FD, Goldie H, Cardemil E (2002). "Ligand interactions and protein conformational changes of phosphopyridoxyl-labeled Escherichia coli phosphoenolpyruvate carboxykinase determined by fluorescence spectroscopy." Eur J Biochem 269(20);4960-8. PMID: 12383254

Encinas93: Encinas MV, Rojas MC, Goldie H, Cardemil E (1993). "Comparative steady-state fluorescence studies of cytosolic rat liver (GTP), Saccharomyces cerevisiae (ATP) and Escherichia coli (ATP) phospho enol pyruvate carboxykinases." Biochim Biophys Acta 1162(1-2);195-202. PMID: 8448184

Encinas95: Encinas MV, Olsen LR, Diaz JF, Andreu JM, Goldie H, Cardemil E (1995). "Circular dichroism and Fourier transform infrared spectroscopic studies on the secondary structure of Saccharomyces cerevisiae and Escherichia coli phospho enolpyruvate carboxykinases." Biochim Biophys Acta 1252(1);23-7. PMID: 7548162

Encinas98: Encinas MV, Evangelio JA, Andreu JM, Goldie H, Cardemil E (1998). "Stability of Escherichia coli phosphoenolpyruvate carboxykinase against urea-induced unfolding and ligand effects." Eur J Biochem 255(2);439-45. PMID: 9716386

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

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."

Goldie80: Goldie AH, Sanwal BD (1980). "Genetic and physiological characterization of Escherichia coli mutants deficient in phosphoenolpyruvate carboxykinase activity." J Bacteriol 141(3);1115-21. PMID: 6988403

Goldie80a: Goldie AH, Sanwal BD (1980). "Allosteric control by calcium and mechanism of desensitization of phosphoenolpyruvate carboxykinase of Escherichia coli." J Biol Chem 1980;255(4);1399-405. PMID: 6986370

Goldie81: Goldie AH, Sanwal BD (1981). "Temperature-sensitive mutation affecting synthesis of phosphoenolpyruvate carboxykinase in Escherichia coli." J Bacteriol 148(2);720-3. PMID: 7028726

Goldie84: Goldie H (1984). "Regulation of transcription of the Escherichia coli phosphoenolpyruvate carboxykinase locus: studies with pck-lacZ operon fusions." J Bacteriol 159(3);832-6. PMID: 6434512

Goldie90: Goldie H, Medina V (1990). "Physical and genetic analysis of the phosphoenolpyruvate carboxykinase (pckA) locus from Escherichia coli K12." Mol Gen Genet 220(2);191-6. PMID: 2183002

Hansen74: Hansen EJ, Juni E (1974). "Two routes for synthesis of phosphoenolpyruvate from C4-dicarboxylic acids in Escherichia coli." Biochem Biophys Res Commun 59(4);1204-10. PMID: 4370531

Hou95: Hou SY, Chao YP, Liao JC (1995). "A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity." J Bacteriol 177(6);1620-3. PMID: 7883719

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

Krebs76: Krebs A, Bridger WA (1976). "On the monomeric structure and proposed regulatory properties of phosphoenolpyruvate carboxykinase of Escherichia coli." Can J Biochem 54(1);22-6. PMID: 175900

Krebs80: Krebs A, Bridger WA (1980). "The kinetic properties of phosphoenolpyruvate carboxykinase of Escherichia coli." Can J Biochem 1980;58(4);309-18. PMID: 6991069

Lee99a: Lee B, Yen J, Yang L, Liao JC (1999). "Incorporating qualitative knowledge in enzyme kinetic models using fuzzy logic." Biotechnol Bioeng 62(6);722-9. PMID: 9951527

Liao94: Liao JC, Chao YP, Patnaik R (1994). "Alteration of the biochemical valves in the central metabolism of Escherichia coli." Ann N Y Acad Sci 745;21-34. PMID: 7832509

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

Matte96: Matte A, Goldie H, Sweet RM, Delbaere LT (1996). "Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold." J Mol Biol 256(1);126-43. PMID: 8609605

Matte97: Matte A, Tari LW, Goldie H, Delbaere LT (1997). "Structure and mechanism of phosphoenolpyruvate carboxykinase." J Biol Chem 272(13);8105-8. PMID: 9139042

Medina90: Medina V, Pontarollo R, Glaeske D, Tabel H, Goldie H (1990). "Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae." J Bacteriol 172(12);7151-6. PMID: 1701430

Mizuno82: Mizuno T, Wurtzel ET, Inouye M (1982). "Osmoregulation of gene expression. II. DNA sequence of the envZ gene of the ompB operon of Escherichia coli and characterization of its gene product." J Biol Chem 257(22);13692-8. PMID: 6292200

Oh00: Oh MK, Liao JC (2000). "Gene expression profiling by DNA microarrays and metabolic fluxes in Escherichia coli." Biotechnol Prog 16(2);278-86. PMID: 10753455

Pai96: Pai EF (1996). "Familiar jaws with new twists." Nat Struct Biol 3(4);307-9. PMID: 8599751

Peng03: Peng L, Shimizu K (2003). "Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement." Appl Microbiol Biotechnol 61(2);163-78. PMID: 12655459

Romeo93: Romeo T, Gong M, Liu MY, Brun-Zinkernagel AM (1993). "Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties." J Bacteriol 175(15);4744-55. PMID: 8393005

Sabnis95: Sabnis NA, Yang H, Romeo T (1995). "Pleiotropic regulation of central carbohydrate metabolism in Escherichia coli via the gene csrA." J Biol Chem 1995;270(49);29096-104. PMID: 7493933

Sudom01: Sudom AM, Prasad L, Goldie H, Delbaere LT (2001). "The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3)." J Mol Biol 314(1);83-92. PMID: 11724534

Sudom03: Sudom A, Walters R, Pastushok L, Goldie D, Prasad L, Delbaere LT, Goldie H (2003). "Mechanisms of activation of phosphoenolpyruvate carboxykinase from Escherichia coli by Ca2+ and of desensitization by trypsin." J Bacteriol 185(14);4233-42. PMID: 12837799

Tari96: Tari LW, Matte A, Pugazhenthi U, Goldie H, Delbaere LT (1996). "Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase." Nat Struct Biol 3(4);355-63. PMID: 8599762

Tari97: Tari LW, Matte A, Goldie H, Delbaere LT (1997). "Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions." Nat Struct Biol 4(12);990-4. PMID: 9406547

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt14: UniProt Consortium (2014). "UniProt version 2014-01 released on 2014-01-01 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."

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

Wright69: Wright JA, Sanwal BD (1969). "Regulatory mechanisms involving nicotinamide adenine nucleotides as all teric effectors. II. Control of phosphoenolpyruvate carboxykinase." J Biol Chem 244(7);1838-45. PMID: 4388616

Zhang09a: 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

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

Nakano14: Nakano M, Ogasawara H, Shimada T, Yamamoto K, Ishihama A (2014). "Involvement of cAMP-CRP in transcription activation and repression of the pck gene encoding PEP carboxykinase, the key enzyme of gluconeogenesis." FEMS Microbiol Lett 355(2);93-9. PMID: 24814025

Prost99: Prost JF, Cozzone AJ (1999). "Detection of an extended-10 element in the promoter region of the pckA gene encoding phosphoenolpyruvate carboxykinase in Escherichia coli." Biochimie 1999;81(3);197-200. PMID: 10385000

Ramseier95: Ramseier TM, Bledig S, Michotey V, Feghali R, Saier MH (1995). "The global regulatory protein FruR modulates the direction of carbon flow in Escherichia coli." Mol Microbiol 1995;16(6);1157-69. PMID: 8577250


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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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