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Escherichia coli K-12 substr. MG1655 Enzyme: pyruvate kinase I



Gene: pykF Accession Numbers: EG10804 (EcoCyc), b1676, ECK1672

Synonyms: type I pyruvate kinase, pyruvate kinase type F

Regulation Summary Diagram: ?

Regulation summary diagram for pykF

Subunit composition of pyruvate kinase I = [PykF]4
         pyruvate kinase I monomer = PykF

Summary:
Pyruvate kinase is a key allosteric enzyme of glycolysis, catalyzing one of the two substrate-level phosphorylation steps that generate ATP. The second product, pyruvate, is either used in many metabolic pathways to synthesize cell materials, or is further oxidized via the TCA cycle. The transfer of the phosphoryl group of phosphoenolpyruvate to ADP to form pyruvate and ATP is the last step in the glycolytic pathway and is irreversible under physiological conditions [Valentini00, Mattevi95].

Two forms of pyruvate kinase have been described in E. coli. Pyruvate kinase I encoded by pykF and pyruvate kinase II encoded by pykA differ in physical and chemical properties as well as in their kinetic behavior. Although the two enzymes are under independent genetic control, they do coexist in a wide range of nutritional and metabolic states [Malcovati73, Gibriel75, Valentini79, Malcovati82, GarridoPertierr83, Valentini93, Ponce95].

The two enzymes are not interchangeable. Both show positive cooperative effects with respect to their substrate phosphoenolpyruvate, although pyruvate kinase II shows only limited cooperativity. Pyruvate kinase I is activated by fructose 1,6-bisphosphate and inhibited by ATP and succinyl-CoA, whereas pyruvate kinase II is allosterically activated by AMP and several sugar phosphates. Both enzymes are homotetramers [Waygood75, Mort78, Somani77, Valentini79, Malcovati82, Valentini91].

Pyruvate kinase I has been purified and characterized from cell extracts of E. coli K-12 [Waygood74, Waygood76], and recombinant enzyne has been overproduced and characterized [Valentini00]. A detailed kinetic analysis of pyruvate kinase I demonstrated the dependence of the reaction rate on the concentrations of various substrates, and the resulting sigmoid or hyperbolic curves. Several conformational states of the enzyme were defined [Markus80, Boiteux83].

The crystal structure of E. coli pyruvate kinase I has been determined at 2.50 Å resolution. Crystal structures of mutants R292D and R271L have also been determined at 1.80 Å and 2.80 Å resolution, respectively. The data suggested that during the quaternary structure transition from the inactive T-state to the active R-state the 12 domains of the tetramer change orientation. The domain interfaces couple changes in tertiary and quaternary structure to alterations in the fructose 1,6-bisphosphate and substrate binding sites [Mattevi95, Valentini00].

The oligomeric state of pyruvate kinase I in the presence of different allosteric effectors was investigated using steady-state kinetics. Analytical ultracentrifugation with fluorescence monitoring allowed detection of the enzyme at low nanomolar concentrations. The results showed that the dissociation constant is very low and that neither the substrates nor the allosteric effector affected the tetrameric state [Zhu10].

A free N-terminal amino acid can be detected in both forms of pyruvate kinase; it corresponds to methionine for type I and serine for type II [Malcovati82]. Comparison with the known primary structures shows that bacterial enzymes lack a substantial portion of the N-terminal sequence with respect to pyruvate kinases from vertebrates [Valentini91].

Genes pykF and pykA are often used in metabolic engineering due to their importance in the control of metabolic flux in glycolysis. In various strains of E. coli the effects of single and double mutants of pykF and pykA on gene expression levels, enzyme activities, metabolite concentrations, glycolytic flux, and the production of useful compounds have been studied [Ponce, Gosset96, Ponce99, Zhu, Emmerling02, Siddiquee04, Al04, Ponce05, Sabido14, Zhang11a, Meza12, Peskov12, Soellner13, Rodriguez13, Weiner14]. Single and double knockouts of genes pykF and pykA can also affect plasmid DNA synthesis and cyclic AMP levels [Goncalves13, Wunderlich14].

Regulation of pykF by FruR in response to carbon source has been described [Bledig96]. A mutant in the carbon storage regulator gene csrA is deficient in pyruvate kinase I activity as well as some other glycolytic enzymes, but is not deficient in pyruvate kinase II activity [Sabnis95].

pykF shows differential codon adaptation, resulting in differential translation efficiency signatures, in thermophilic microbes. It was therefore predicted to play a role in the heat shock response. A pykF deletion mutant was shown to be more sensitive than wild-type specifically to heat shock, but not other stresses [Krisko14].

PykF: "pyruvate kinase, fructose 1,6-diphosphate-activated" [Kornberg73]

Review: [Munoz03]

Locations: cytosol, membrane

Map Position: [1,753,722 -> 1,755,134] (37.8 centisomes, 136°)
Length: 1413 bp / 470 aa

Molecular Weight of Polypeptide: 50.729 kD (from nucleotide sequence), 60.0 kD (experimental) [Waygood74 ]

Molecular Weight of Multimer: 240.0 kD (experimental) [Waygood74]

pI: 6.08

Isozyme Sequence Similarity [Muirhead90]:

Unification Links: ASAP:ABE-0005600 , CGSC:17620 , DIP:DIP-36221N , EchoBASE:EB0797 , EcoGene:EG10804 , EcoliWiki:b1676 , ModBase:P0AD61 , OU-Microarray:b1676 , PortEco:pykF , PR:PRO_000023656 , Pride:P0AD61 , Protein Model Portal:P0AD61 , RefSeq:NP_416191 , RegulonDB:EG10804 , SMR:P0AD61 , String:511145.b1676 , Swiss-Model:P0AD61 , UniProt:P0AD61

Relationship Links: InterPro:IN-FAMILY:IPR001697 , InterPro:IN-FAMILY:IPR011037 , InterPro:IN-FAMILY:IPR015793 , InterPro:IN-FAMILY:IPR015794 , InterPro:IN-FAMILY:IPR015795 , InterPro:IN-FAMILY:IPR015806 , InterPro:IN-FAMILY:IPR015813 , InterPro:IN-FAMILY:IPR018209 , Panther:IN-FAMILY:PTHR11817 , PDB:Structure:1E0T , PDB:Structure:1E0U , PDB:Structure:1PKY , Pfam:IN-FAMILY:PF00224 , Pfam:IN-FAMILY:PF02887 , Prints:IN-FAMILY:PR01050 , Prosite:IN-FAMILY:PS00110

In Paralogous Gene Group: 354 (3 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for pykF

GO Terms:

Biological Process: GO:0006096 - glycolytic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA01a, Ponce95]
GO:0009408 - response to heat Inferred from experiment [Krisko14]
GO:0051289 - protein homotetramerization Inferred from experiment [Valentini79]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0004743 - pyruvate kinase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Valentini00, Waygood74]
GO:0042802 - identical protein binding Inferred from experiment [Valentini79]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA01a]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0030955 - potassium ion 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, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]

MultiFun Terms: metabolism energy metabolism, carbon fermentation
metabolism energy metabolism, carbon glycolysis

Essentiality data for pykF 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]

Credits:
Last-Curated ? 24-Feb-2015 by Fulcher C , SRI International


Enzymatic reaction of: pyruvate kinase

Synonyms: pyruvate kinase, phosphoenolpyruvate kinase, phosphoenol transphosphorylase, pyruvate 2-0-phosphotransferase

EC Number: 2.7.1.40

ADP + phosphoenolpyruvate + H+ <=> pyruvate + ATP

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.

Alternative Substrates for ADP: IDP [Waygood74 ] , CDP [Waygood74 ] , GDP [Waygood74 ] , UDP [Waygood74 ]

In Pathways: superpathway of hexitol degradation (bacteria) , superpathway of glycolysis and Entner-Doudoroff , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , mixed acid fermentation , glycolysis II (from fructose 6-phosphate) , glycolysis I (from glucose 6-phosphate)

Summary:
The enzyme requires both divalent (Mg2+, Mn2+) and monovalent (K+) cations. The 5'-diphosphates of guanosine, inosine, uridine and cytidine can also serve as phospho acceptors [Muirhead90, Waygood74].

Cofactors or Prosthetic Groups [Comment 5]: K+ [Muirhead90], Mg2+ [Muirhead90]

Alternative Cofactors for Mg2+ [Boiteux83 ]: Mn2+

Activators (Allosteric): fructose 1,6-bisphosphate [Markus80]

Activators (Unknown Mechanism): Ca2+ [Boiteux83, Comment 6]

Inhibitors (Unknown Mechanism): GTP [Waygood74] , ATP [Speranza89, Waygood74, Comment 7] , succinyl-CoA [Speranza89, Waygood74, Comment 7] , Ca2+ [Speranza89, Comment 7]

Primary Physiological Regulators of Enzyme Activity: fructose 1,6-bisphosphate


Sequence Features

Protein sequence of pyruvate kinase I monomer with features indicated

Feature Class Location Citations Comment
Amino-Acid-Sites-That-Bind 32
[UniProt10a]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 34
[UniProt10a]
UniProt: Potassium; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 36
[UniProt10a]
UniProt: Potassium; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 44
[Valentini91, UniProt10]
UniProt: (in Ref. 6; AA sequence);
Metal-Binding-Site 66
[UniProt10a]
UniProt: Potassium; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 67
[UniProt10a]
UniProt: Potassium; Non-Experimental Qualifier: by similarity;
N6-acetyllysine-Modification 76
[Zhang09a, UniProt15]
UniProt: N6-acetyllysine.
Amino-Acid-Site 220
[UniProt10a]
UniProt: Transition state stabilizer; Sequence Annotation Type: site; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 222
[UniProt10a]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 245
[UniProt10a]
UniProt: Substrate; via amide nitrogen; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 246
[UniProt10a]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 278
[UniProt10a]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
N6-acetyllysine-Modification 319
[Zhang09a, UniProt15]
UniProt: N6-acetyllysine.
Sequence-Conflict 379
[Speranza89, UniProt10]
UniProt: (in Ref. 8; AA sequence);
Sequence-Conflict 401
[Speranza89, UniProt10]
UniProt: (in Ref. 8; AA sequence);
Sequence-Conflict 451 -> 470
[Ohara89, Aiba96, UniProt10]
UniProt: (in Ref. 1 and 3);


Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Notes:

History:
10/20/97 Gene b1676 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10804; confirmed by SwissProt match.


References

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Al04: Al Zaid Siddiquee K, Arauzo-Bravo MJ, Shimizu K (2004). "Metabolic flux analysis of pykF gene knockout Escherichia coli based on 13C-labeling experiments together with measurements of enzyme activities and intracellular metabolite concentrations." Appl Microbiol Biotechnol 63(4);407-17. PMID: 12802531

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

Bledig96: Bledig SA, Ramseier TM, Saier MH (1996). "Frur mediates catabolite activation of pyruvate kinase (pykF) gene expression in Escherichia coli." J Bacteriol 178(1);280-3. PMID: 8550429

Boiteux83: Boiteux A, Markus M, Plesser T, Hess B, Malcovati M (1983). "Analysis of progress curves. Interaction of pyruvate kinase from Escherichia coli with fructose 1,6-bisphosphate and calcium ions." Biochem J 1983;211(3);631-40. PMID: 6349612

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

Emmerling02: Emmerling M, Dauner M, Ponti A, Fiaux J, Hochuli M, Szyperski T, Wuthrich K, Bailey JE, Sauer U (2002). "Metabolic flux responses to pyruvate kinase knockout in Escherichia coli." J Bacteriol 184(1);152-64. PMID: 11741855

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

GarridoPertierr83: Garrido-Pertierra A, Cooper RA (1983). "Evidence for two distinct pyruvate kinase genes in Escherichia coli K-12." FEBS Lett 1983;162(2);420-2. PMID: 6354749

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

Gibriel75: Gibriel AY, Doelle HW (1975). "Investigation into pyruvate kinases from Escherichia coli K-12 grown under aerobic and anaerobic conditions." Microbios 12(50);179-97. PMID: 1099402

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."

Goncalves13: Goncalves GA, Prazeres DM, Monteiro GA, Prather KL (2013). "De novo creation of MG1655-derived E. coli strains specifically designed for plasmid DNA production." Appl Microbiol Biotechnol 97(2);611-20. PMID: 22885693

Gosset96: Gosset G, Yong-Xiao J, Berry A (1996). "A direct comparison of approaches for increasing carbon flow to aromatic biosynthesis in Escherichia coli." J Ind Microbiol 17(1);47-52. PMID: 8987689

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

Kornberg73: Kornberg HL, Malcovati M (1973). "Control in situ of the pyruvate kinase activity of Escherichia coli." FEBS Lett 32(2);257-9. PMID: 4582155

Krisko14: Krisko A, Copi T, Gabaldon T, Lehner B, Supek F (2014). "Inferring gene function from evolutionary change in signatures of translation efficiency." Genome Biol 15(3);R44. PMID: 24580753

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

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

Malcovati73: Malcovati M, Valentini G, Kornberg HL (1973). "Two forms of pyruvate kinase in E. coli: their properties and regulation." Acta Vitaminol Enzymol 27(1);96-111. PMID: 4584473

Malcovati82: Malcovati M, Valentini G (1982). "AMP- and fructose 1,6-bisphosphate-activated pyruvate kinases from Escherichia coli." Methods Enzymol 1982;90 Pt E;170-9. PMID: 6759852

Markus80: Markus M, Plesser T, Boiteux A, Hess B, Malcovati M (1980). "Analysis of progress curves. Rate law of pyruvate kinase type I from Escherichia coli." Biochem J 1980;189(3);421-33. PMID: 7011316

Mattevi95: Mattevi A, Valentini G, Rizzi M, Speranza ML, Bolognesi M, Coda A (1995). "Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition." Structure 3(7);729-41. PMID: 8591049

Meza12: Meza E, Becker J, Bolivar F, Gosset G, Wittmann C (2012). "Consequences of phosphoenolpyruvate:sugar phosphotranferase system and pyruvate kinase isozymes inactivation in central carbon metabolism flux distribution in Escherichia coli." Microb Cell Fact 11;127. PMID: 22973998

Mort78: Mort JS, Sanwal BD (1978). "The control of pyruvate kinases of Escherichia coli: further studies of the enzyme activated by ribose-5-phosphate." Can J Biochem 56(6);647-53. PMID: 27294

Muirhead90: Muirhead H (1990). "Isoenzymes of pyruvate kinase." Biochem Soc Trans 1990;18(2);193-6. PMID: 2379684

Munoz03: Munoz ME, Ponce E (2003). "Pyruvate kinase: current status of regulatory and functional properties." Comp Biochem Physiol B Biochem Mol Biol 135(2);197-218. PMID: 12798932

Ohara89: Ohara O, Dorit RL, Gilbert W (1989). "Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli." Proc Natl Acad Sci U S A 86(18);6883-7. PMID: 2674937

Peskov12: Peskov K, Mogilevskaya E, Demin O (2012). "Kinetic modelling of central carbon metabolism in Escherichia coli." FEBS J 279(18);3374-85. PMID: 22823407

Ponce: Ponce E, Martinez A, Bolivar F, Valle F (1998). "Stimulation of glucose catabolism through the pentose pathway by the absence of the two pyruvate kinase isoenzymes in Escherichia coli." Biotechnol Bioeng 58(2-3);292-5. PMID: 10191403

Ponce05: Ponce E, Garcia M, Munoz ME (2005). "Participation of the Entner-Doudoroff pathway in Escherichia coli strains with an inactive phosphotransferase system (PTS- Glc+) in gluconate and glucose batch cultures." Can J Microbiol 51(11);975-82. PMID: 16333337

Ponce95: Ponce E, Flores N, Martinez A, Valle F, Bolivar F (1995). "Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: the relative roles of these enzymes in pyruvate biosynthesis." J Bacteriol 177(19);5719-22. PMID: 7559366

Ponce99: Ponce E (1999). "Effect of growth rate reduction and genetic modifications on acetate accumulation and biomass yields in Escherichia coli." J Biosci Bioeng 87(6);775-80. PMID: 16232553

Rodriguez13: Rodriguez A, Martinez JA, Baez-Viveros JL, Flores N, Hernandez-Chavez G, Ramirez OT, Gosset G, Bolivar F (2013). "Constitutive expression of selected genes from the pentose phosphate and aromatic pathways increases the shikimic acid yield in high-glucose batch cultures of an Escherichia coli strain lacking PTS and pykF." Microb Cell Fact 12;86. PMID: 24079972

Sabido14: Sabido A, Sigala JC, Hernandez-Chavez G, Flores N, Gosset G, Bolivar F (2014). "Physiological and transcriptional characterization of Escherichia coli strains lacking interconversion of phosphoenolpyruvate and pyruvate when glucose and acetate are coutilized." Biotechnol Bioeng 111(6);1150-60. PMID: 24375081

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

Siddiquee04: Siddiquee KA, Arauzo-Bravo MJ, Shimizu K (2004). "Effect of a pyruvate kinase (pykF-gene) knockout mutation on the control of gene expression and metabolic fluxes in Escherichia coli." FEMS Microbiol Lett 235(1);25-33. PMID: 15158258

Soellner13: Soellner S, Rahnert M, Siemann-Herzberg M, Takors R, Altenbuchner J (2013). "Evolution of pyruvate kinase-deficient Escherichia coli mutants enables glycerol-based cell growth and succinate production." J Appl Microbiol 115(6);1368-78. PMID: 23957584

Somani77: Somani BL, Valentini G, Malcovati M (1977). "Purification and molecular properties of the AMP-activated pyruvate kinase from Escherichia coli." Biochim Biophys Acta 482(1);52-63. PMID: 193572

Speranza89: Speranza ML, Valentini G, Iadarola P, Stoppini M, Malcovati M, Ferri G (1989). "Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli." Biol Chem Hoppe Seyler 1989;370(3);211-6. PMID: 2653362

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.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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."

Valentini00: Valentini G, Chiarelli L, Fortin R, Speranza ML, Galizzi A, Mattevi A (2000). "The allosteric regulation of pyruvate kinase." J Biol Chem 275(24);18145-52. PMID: 10751408

Valentini79: Valentini G, Iadarola P, Somani BL, Malcovati M (1979). "Two forms of pyruvate kinase in Escherichia coli. A comparison of chemical and molecular properties." Biochim Biophys Acta 570(2);248-58. PMID: 387087

Valentini91: Valentini G, Stoppini M, Speranza ML, Malcovati M, Ferri G (1991). "Bacterial pyruvate kinases have a shorter N-terminal domain." Biol Chem Hoppe Seyler 1991;372(2);91-3. PMID: 1859631

Valentini93: Valentini G, Stoppini M, Iadarola P, Malcovati M, Ferri G, Speranza ML (1993). "Divergent binding sites in pyruvate kinases I and II from Escherichia coli." Biol Chem Hoppe Seyler 374(1);69-74. PMID: 8439398

Waygood74: Waygood EB, Sanwal BD (1974). "The control of pyruvate kinases of Escherichia coli. I. Physicochemical and regulatory properties of the enzyme activated by fructose 1,6-diphosphate." J Biol Chem 249(1);265-74. PMID: 4588693

Waygood75: Waygood EB, Rayman MK, Sanwal BD (1975). "The control of pyruvate kinases of Escherichia coli. II. Effectors and regulatory properties of the enzyme activated by ribose 5-phosphate." Can J Biochem 53(4);444-54. PMID: 236081

Waygood76: Waygood EB, Mort JS, Sanwal BD (1976). "The control of pyruvate kinase of Escherichia coli. Binding of substrate and allosteric effectors to the enzyme activated by fructose 1,6-bisphosphate." Biochemistry 15(2);277-82. PMID: 764863

Weiner14: Weiner M, Trondle J, Albermann C, Sprenger GA, Weuster-Botz D (2014). "Carbon storage in recombinant Escherichia coli during growth on glycerol and lactic acid." Biotechnol Bioeng 111(12);2508-19. PMID: 24902947

Wunderlich14: Wunderlich M, Taymaz-Nikerel H, Gosset G, Ramirez OT, Lara AR (2014). "Effect of growth rate on plasmid DNA production and metabolic performance of engineered Escherichia coli strains." J Biosci Bioeng 117(3);336-42. PMID: 24012107

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

Zhang11a: Zhang X, Wang X, Shanmugam KT, Ingram LO (2011). "L-malate production by metabolically engineered Escherichia coli." Appl Environ Microbiol 77(2);427-34. PMID: 21097588

Zhu: Zhu T, Phalakornkule C, Koepsel RR, Domach MM, Ataai MM (2001). "Cell growth and by-product formation in a pyruvate kinase mutant of E. coli." Biotechnol Prog 17(4);624-8. PMID: 11485421

Zhu10: Zhu T, Bailey MF, Angley LM, Cooper TF, Dobson RC (2010). "The quaternary structure of pyruvate kinase type 1 from Escherichia coli at low nanomolar concentrations." Biochimie 92(1);116-20. PMID: 19800933

Other References Related to Gene Regulation

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

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

Olvera09: Olvera L, Mendoza-Vargas A, Flores N, Olvera M, Sigala JC, Gosset G, Morett E, Bolivar F (2009). "Transcription analysis of central metabolism genes in Escherichia coli. Possible roles of sigma38 in their expression, as a response to carbon limitation." PLoS One 4(10);e7466. PMID: 19838295


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Jul 3, 2015, biocyc13.