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Escherichia coli K-12 substr. MG1655 Enzyme: 6-phosphofructokinase I



Gene: pfkA Accession Numbers: EG10699 (EcoCyc), b3916, ECK3908

Synonyms: PFK I

Regulation Summary Diagram: ?

Regulation summary diagram for pfkA

Subunit composition of 6-phosphofructokinase I = [PfkA]4
         6-phosphofructokinase-1 monomer = PfkA

Summary:
6-phosphofructokinase I (PFK I) catalyzes the phosphorylation of fructose-6-phosphate and is a key enzyme regulating the glycolysis pathway. The enzyme can not catalyze the reverse reaction in vivo.

E. coli contains two PFK isozymes, PFK I and PFK II, which do not share sequence similarity [Hellinga85]. More than 90% of the phosphofructokinase activity present in wild type E. coli can be attributed to PFK I [Kotlarz75]. The enzyme shows cooperative kinetics with the substrate fructose-6-phosphate, but not with the other substrate, ATP [Blangy68, Hellinga85].

The active site, kinetic mechanism, pH dependence, allosteric properties, and effector binding sites of the enzyme have been studied in depth. Mutants in the active site that change cooperativity have been generated [Berger90, Auzat94]. pH affects both cooperativity and maximum velocity of the enzyme [DevilleBonne91a, Zheng94, Zheng95]. Also see publications on the kinetic mechanism [Hellinga, Berger91, DevilleBonne91, Laine92, Berger92, Johnson92, Zheng92a, Johnson94a, Johnson94, Zheng94a, Wang98a, Wang99, Wang01, Fenton03a], allosteric properties [Le82, Serre90, DevilleBonne92, Auzat95a, Auzat95, Auzat95b, Auzat97, Johnson97, Pham01a, Johnson01, Fenton02, Fenton03, Pham03, Fenton04, Fenton09], and the effector binding site [Kundrot91, Lau, Lau87, Lau89, Auzat94a, Pham01, Pham01b]. A kinetic model of the enzyme has been constructed [Peskov08a]. The folding and subunit association pathway of E. coli Pfk I has also been studied [Bras89].

Crystal structures of PFK I have been solved with and without activators and inhibitors [Rypniewski89, Shirakihara88].

Recently, it was shown that PFK I also catalyzes phosphorylation of sedoheptulose-7-phosphate as part of the sedoheptulose bisphosphate bypass [Nakahigashi09].

Based on sequence similarity, PfkA was predicted to be an NAD+ kinase [Reed03].

In metabolic engineering applications a ΔpfkA strain was found to increase NADPH generation by directing fructose-6-phosphate oxidation to the pentose phosphate pathway [Siedler12, Wang13, Siedler14]. A strategy for the production of D-glucose from pentoses included a pfkA knockout strain [Xia15]. A strategy for the production of myo-inositol involved dynamic knockdown of Pfk-I levels [Brockman15].

Useful hosts and expression vectors for studying E. coli phosphofructokinase have been developed [Lovingshimer06, Tie12]. A series of vectors inducibly expressing paired-terminus antisense RNAs has been constructed to silence central carbon metabolism in host E. coli K-12 MG1655. A vector that silenced pfkA at 87% efficacy resulted in a defect in carbon catabolite repression [Nakashima14].

PfkA: "phosphofructokinase A"

Locations: cytosol

Map Position: [4,105,575 -> 4,106,537] (88.49 centisomes, 319°)
Length: 963 bp / 320 aa

Molecular Weight of Polypeptide: 34.842 kD (from nucleotide sequence), 35.0 kD (experimental) [Blangy68a ]

Molecular Weight of Multimer: 142.0 kD (experimental) [Blangy68a]

pI: 5.32

Unification Links: ASAP:ABE-0012789 , CGSC:413 , DIP:DIP-35841N , EchoBASE:EB0693 , EcoGene:EG10699 , EcoliWiki:b3916 , Mint:MINT-1322275 , ModBase:P0A796 , OU-Microarray:b3916 , PortEco:pfkA , PR:PRO_000023514 , Pride:P0A796 , Protein Model Portal:P0A796 , RefSeq:NP_418351 , RegulonDB:EG10699 , SMR:P0A796 , String:511145.b3916 , UniProt:P0A796

Relationship Links: InterPro:IN-FAMILY:IPR000023 , InterPro:IN-FAMILY:IPR012003 , InterPro:IN-FAMILY:IPR012828 , InterPro:IN-FAMILY:IPR015912 , InterPro:IN-FAMILY:IPR022953 , PDB:Structure:1PFK , PDB:Structure:2PFK , Pfam:IN-FAMILY:PF00365 , Prints:IN-FAMILY:PR00476 , Prosite:IN-FAMILY:PS00433

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for pfkA

GO Terms:

Biological Process: GO:0006007 - glucose catabolic process Inferred from experiment [Morrissey68]
GO:0006096 - glycolytic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06, GOA01a, Roehl76, Itoh04]
GO:0044275 - cellular carbohydrate catabolic process Inferred from experiment [Morrissey68]
GO:0046835 - carbohydrate phosphorylation Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Blangy68, Vinopal75]
GO:0051289 - protein homotetramerization Inferred from experiment [Blangy68a]
GO:0006002 - fructose 6-phosphate metabolic process Inferred by computational analysis [GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment [Johnson92]
GO:0003872 - 6-phosphofructokinase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Blangy68, Vinopal75]
GO:0005524 - ATP binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Auzat94]
GO:0019003 - GDP binding Inferred from experiment [Kotlarz77]
GO:0032553 - ribonucleotide binding Inferred from experiment [Blangy68]
GO:0042802 - identical protein binding Inferred from experiment [Blangy68a]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a]
GO:0003951 - NAD+ kinase activity Inferred by computational analysis [Reed03]
GO:0008443 - phosphofructokinase activity Inferred by computational analysis [GOA01a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, Blangy68]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005945 - 6-phosphofructokinase complex Inferred from experiment [Martel84]

MultiFun Terms: metabolism carbon utilization carbon compounds

Essentiality data for pfkA 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 Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
No [Feist07, Comment 3]

Credits:
Curated 24-Sep-2010 by Keseler I , SRI International
Last-Curated ? 07-May-2015 by Fulcher C , SRI International


Enzymatic reaction of: sedoheptulose-7-phosphate kinase (6-phosphofructokinase I)

D-sedoheptulose 7-phosphate + ATP <=> D-sedoheptulose-1,7-bisphosphate + ADP + H+

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: sedoheptulose bisphosphate bypass


Enzymatic reaction of: 6-phosphofructokinase

Synonyms: fructose-6-p-1-kinase, fructose-6-phosphate-1-phosphotransferase

EC Number: 2.7.1.11

β-D-fructofuranose 6-phosphate + ATP <=> ADP + fructose 1,6-bisphosphate + H+

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. [Babul78]

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

Summary:
Catalytic properties of phosphofructokinase were initially studied using the enzyme from E. coli B, e.g. by [ATKINSON65].

The enzyme is able to catalyze the reverse reaction, synthesis of ATP, in vitro, but not in vivo [Babul78, Auzat92].

Cofactors or Prosthetic Groups: Mg2+ [Blangy68]

Cofactor Binding Comment: The binding sites have been identified in the crystalline structure.[Rypniewski89, DevilleBonne91a]

Activators (Allosteric): GDP [Blangy68] , ADP [Blangy68]

Activators (Non-Allosteric): β-D-fructofuranose 6-phosphate [Fraenkel73]

Inhibitors (Allosteric): phosphoenolpyruvate [Fraenkel73, Blangy68]

Primary Physiological Regulators of Enzyme Activity: GDP , ADP , phosphoenolpyruvate

Kinetic Parameters:

Substrate
Km (μM)
Citations
β-D-fructofuranose 6-phosphate
30.0
[Berger91]
ATP
60.0
[Blangy68]


Sequence Features

Protein sequence of 6-phosphofructokinase-1 monomer with features indicated

Feature Class Location Attached Group Citations Comment
Amino-Acid-Sites-That-Bind 12  
[UniProt15]
UniProt: ATP; via amide nitrogen.
Protein-Segment 22 -> 26  
[UniProt15]
UniProt: Allosteric activator ADP binding; shared with dimeric partner; Sequence Annotation Type: region of interest.
Protein-Segment 55 -> 60  
[UniProt14]
UniProt: Allosteric activator ADP binding; shared with dimeric partner; Sequence Annotation Type: region of interest.
Nucleotide-Phosphate-Binding-Region 73 -> 74 ATP
[UniProt15]
UniProt: ATP.
Sequence-Conflict 74  
[Hellinga85, UniProt10a]
UniProt: (in Ref. 1; CAA26356);
Nucleotide-Phosphate-Binding-Region 103 -> 106 ATP
[UniProt15]
UniProt: ATP.
Sequence-Conflict 103 -> 104  
[Hellinga85, UniProt10a]
UniProt: (in Ref. 1; CAA26356);
Metal-Binding-Site 104  
[Shirakihara88, UniProt14]
UniProt: Magnesium; catalytic.
Protein-Segment 126 -> 128  
[UniProt14]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 128  
[Hellinga, UniProt15]
UniProt: 18000-fold reduction of catalytic rate.
Active-Site 128  
[Shirakihara88, Hellinga, UniProt15]
UniProt: Proton acceptor.
Amino-Acid-Sites-That-Bind 155  
[Shirakihara88, UniProt14]
UniProt: Allosteric activator ADP.
Amino-Acid-Sites-That-Bind 163  
[UniProt15]
UniProt: Substrate; shared with dimeric partner.
Sequence-Conflict 163  
[Hellinga85, UniProt10a]
UniProt: (in Ref. 1; CAA26356);
Protein-Segment 170 -> 172  
[UniProt14]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 172  
[Hellinga, UniProt15]
UniProt: 3.4-fold reduction in turnover numbers.
Protein-Segment 186 -> 188  
[UniProt14]
UniProt: Allosteric activator ADP binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 212  
[UniProt15]
UniProt: Allosteric activator ADP.
Protein-Segment 214 -> 216  
[UniProt14]
UniProt: Allosteric activator ADP binding; Sequence Annotation Type: region of interest.
Amino-Acid-Sites-That-Bind 223  
[UniProt15]
UniProt: Substrate.
Amino-Acid-Sites-That-Bind 244  
[UniProt15]
UniProt: Substrate; shared with dimeric partner.
Protein-Segment 250 -> 253  
[UniProt14]
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Sequence-Conflict 317 -> 319  
[Hellinga85, UniProt10a]
UniProt: (in Ref. 1; CAA26356);


Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Notes:

History:
10/20/97 Gene b3916 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10699; confirmed by SwissProt match.


References

ATKINSON65: Atkinson DE, Walton GM (1965). "Kinetics of regulatory enzymes. Escherichia coli phosphofructokinase." J Biol Chem 240;757-63. PMID: 14275132

Auzat92: Auzat I, Garel JR (1992). "pH dependence of the reverse reaction catalyzed by phosphofructokinase I from Escherichia coli: implications for the role of Asp 127." Protein Sci 1(2);254-8. PMID: 1304907

Auzat94: Auzat I, Le Bras G, Garel JR (1994). "The cooperativity and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP." Proc Natl Acad Sci U S A 91(12);5242-6. PMID: 8202475

Auzat94a: Auzat I, Le Bras G, Branny P, De La Torre F, Theunissen B, Garel JR (1994). "The role of Glu187 in the regulation of phosphofructokinase by phosphoenolpyruvate." J Mol Biol 235(1);68-72. PMID: 7904653

Auzat95: Auzat I, Byrnes WM, Garel JR, Chang SH (1995). "Role of residue 161 in the allosteric transitions of two bacterial phosphofructokinases." Biochemistry 34(21);7062-8. PMID: 7766616

Auzat95a: Auzat I, Le Bras G, Garel JR (1995). "Hypercooperativity induced by interface mutations in the phosphofructokinase from Escherichia coli." J Mol Biol 246(2);248-53. PMID: 7869376

Auzat95b: Auzat I, Gawlita E, Garel JR (1995). "Slow ligand-induced transitions in the allosteric phosphofructokinase from Escherichia coli." J Mol Biol 249(2);478-92. PMID: 7783204

Auzat97: Auzat I, Le Bras G, Garel JR (1997). "Allosteric activation increases the maximum velocity of E. coli phosphofructokinase." J Mol Biol 267(3);476-80. PMID: 9126831

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

Babul78: Babul J (1978). "Phosphofructokinases from Escherichia coli. Purification and characterization of the nonallosteric isozyme." J Biol Chem 1978;253(12);4350-5. PMID: 149128

Berger90: Berger SA, Evans PR (1990). "Active-site mutants altering the cooperativity of E. coli phosphofructokinase." Nature 343(6258);575-6. PMID: 2137204

Berger91: Berger SA, Evans PR (1991). "Steady-state fluorescence of Escherichia coli phosphofructokinase reveals a regulatory role for ATP." Biochemistry 1991;30(34);8477-80. PMID: 1832014

Berger92: Berger SA, Evans PR (1992). "Site-directed mutagenesis identifies catalytic residues in the active site of Escherichia coli phosphofructokinase." Biochemistry 31(38);9237-42. PMID: 1390710

Blangy68: Blangy D, Buc H, Monod J (1968). "Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli." J Mol Biol 31(1);13-35. PMID: 4229913

Blangy68a: Blangy D (1968). "Phosphofructokinase from E. Coli: Evidence for a tetrameric structure of the enzyme." FEBS Lett 2(2);109-111. PMID: 11946283

Bras89: Bras GL, Teschner W, Deville-Bonne D, Garel JR (1989). "Urea-induced inactivation, dissociation, and unfolding of the allosteric phosphofructokinase from Escherichia coli." Biochemistry 1989;28(17);6836-41. PMID: 2531001

Brockman15: Brockman IM, Prather KL (2015). "Dynamic knockdown of E. coli central metabolism for redirecting fluxes of primary metabolites." Metab Eng 28;104-13. PMID: 25542851

DevilleBonne91: Deville-Bonne D, Laine R, Garel JR (1991). "Substrate antagonism in the kinetic mechanism of E. coli phosphofructokinase-1." FEBS Lett 290(1-2);173-6. PMID: 1833241

DevilleBonne91a: Deville-Bonne D, Bourgain F, Garel JR (1991). "pH dependence of the kinetic properties of allosteric phosphofructokinase from Escherichia coli." Biochemistry 1991;30(23);5750-4. PMID: 1828369

DevilleBonne92: Deville-Bonne D, Garel JR (1992). "A conformational transition involved in antagonistic substrate binding to the allosteric phosphofructokinase from Escherichia coli." Biochemistry 1992;31(6);1695-700. PMID: 1531298

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

Doelle75: Doelle HW (1975). "ATP-sensitive and ATP-insensitive phosphofructokinase in Escherichia coli K-12." Eur J Biochem 50(2);335-42. PMID: 123852

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

Fenton02: Fenton AW, Reinhart GD (2002). "Isolation of a single activating allosteric interaction in phosphofructokinase from Escherichia coli." Biochemistry 41(45);13410-6. PMID: 12416986

Fenton03: Fenton AW, Paricharttanakul NM, Reinhart GD (2003). "Identification of substrate contact residues important for the allosteric regulation of phosphofructokinase from Eschericia coli." Biochemistry 42(21);6453-9. PMID: 12767227

Fenton03a: Fenton AW, Reinhart GD (2003). "Mechanism of substrate inhibition in Escherichia coli phosphofructokinase." Biochemistry 42(43);12676-81. PMID: 14580215

Fenton04: Fenton AW, Paricharttanakul NM, Reinhart GD (2004). "Disentangling the web of allosteric communication in a homotetramer: heterotropic activation in phosphofructokinase from Escherichia coli." Biochemistry 43(44);14104-10. PMID: 15518560

Fenton09: Fenton AW, Reinhart GD (2009). "Disentangling the web of allosteric communication in a homotetramer: heterotropic inhibition in phosphofructokinase from Escherichia coli." Biochemistry 48(51);12323-8. PMID: 19905012

Fraenkel73: Fraenkel DG, Kotlarz D, Buc H (1973). "Two fructose 6-phosphate kinase activities in Escherichia coli." J Biol Chem 248(13);4865-6. PMID: 4268865

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."

Hellinga: Hellinga HW, Evans PR (1987). "Mutations in the active site of Escherichia coli phosphofructokinase." Nature 327(6121);437-9. PMID: 2953977

Hellinga85: Hellinga HW, Evans PR (1985). "Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase." Eur J Biochem 1985;149(2);363-73. PMID: 3158524

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

Itoh04: Itoh A, Ohashi Y, Soga T, Mori H, Nishioka T, Tomita M (2004). "Application of capillary electrophoresis-mass spectrometry to synthetic in vitro glycolysis studies." Electrophoresis 25(13);1996-2002. PMID: 15237399

Johnson01: Johnson JL, Lasagna MD, Reinhart GD (2001). "Influence of a sulfhydryl cross-link across the allosteric-site interface of E. coli phosphofructokinase." Protein Sci 10(11);2186-94. PMID: 11604525

Johnson92: Johnson JL, Reinhart GD (1992). "MgATP and fructose 6-phosphate interactions with phosphofructokinase from Escherichia coli." Biochemistry 31(46);11510-8. PMID: 1445885

Johnson94: Johnson JL, Reinhart GD (1994). "Influence of substrates and MgADP on the time-resolved intrinsic fluorescence of phosphofructokinase from Escherichia coli. Correlation of tryptophan dynamics to coupling entropy." Biochemistry 33(9);2644-50. PMID: 8117727

Johnson94a: Johnson JL, Reinhart GD (1994). "Influence of MgADP on phosphofructokinase from Escherichia coli. Elucidation of coupling interactions with both substrates." Biochemistry 33(9);2635-43. PMID: 8117726

Johnson97: Johnson JL, Reinhart GD (1997). "Failure of a two-state model to describe the influence of phospho(enol)pyruvate on phosphofructokinase from Escherichia coli." Biochemistry 36(42);12814-22. PMID: 9335538

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

Kotlarz75: Kotlarz D, Garreau H, Buc H (1975). "Regulation of the amount and of the activity of phosphofructokinases and pyruvate kinases in Escherichia coli." Biochim Biophys Acta 381(2);257-68. PMID: 122902

Kotlarz77: Kotlarz D, Buc H (1977). "Two Escherichia coli fructose-6-phosphate kinases. Preparative purification, oligomeric structure and immunological studies." Biochim Biophys Acta 484(1);35-48. PMID: 70226

Kundrot91: Kundrot CE, Evans PR (1991). "Designing an allosterically locked phosphofructokinase." Biochemistry 30(6);1478-84. PMID: 1825177

Laine92: Laine R, Deville-Bonne D, Auzat I, Garel JR (1992). "Interaction between the carboxyl groups of Asp127 and Asp129 in the active site of Escherichia coli phosphofructokinase." Eur J Biochem 207(3);1109-14. PMID: 1386803

Lau: Lau FT, Fersht AR (1987). "Conversion of allosteric inhibition to activation in phosphofructokinase by protein engineering." Nature 326(6115);811-2. PMID: 2952886

Lau87: Lau FT, Fersht AR, Hellinga HW, Evans PR (1987). "Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase." Biochemistry 26(13);4143-8. PMID: 2958087

Lau89: Lau FT, Fersht AR (1989). "Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesis." Biochemistry 28(17);6841-7. PMID: 2531002

Le82: Le Bras G, Garel JR (1982). "A proteolyzed derivative of Escherichia coli phosphofructokinase is no longer sensitive to allosteric effectors and still shows cooperativity in substrate binding." Biochemistry 21(26);6656-60. PMID: 6218818

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

Lovingshimer06: Lovingshimer MR, Siegele D, Reinhart GD (2006). "Construction of an inducible, pfkA and pfkB deficient strain of Escherichia coli for the expression and purification of phosphofructokinase from bacterial sources." Protein Expr Purif 46(2);475-82. PMID: 16289704

Martel84: Martel A, Garel JR (1984). "Renaturation of the allosteric phosphofructokinase from Escherichia coli." J Biol Chem 259(8);4917-21. PMID: 6232272

Morrissey68: Morrissey AT, Fraenkel DG (1968). "Selection of fructose 6-phosphate kinase mutants in Escherichia coli." Biochem Biophys Res Commun 32(3);467-73. PMID: 4299078

Nakahigashi09: Nakahigashi K, Toya Y, Ishii N, Soga T, Hasegawa M, Watanabe H, Takai Y, Honma M, Mori H, Tomita M (2009). "Systematic phenome analysis of Escherichia coli multiple-knockout mutants reveals hidden reactions in central carbon metabolism." Mol Syst Biol 5;306. PMID: 19756045

Nakashima14: Nakashima N, Ohno S, Yoshikawa K, Shimizu H, Tamura T (2014). "A vector library for silencing central carbon metabolism genes with antisense RNAs in Escherichia coli." Appl Environ Microbiol 80(2);564-73. PMID: 24212579

Peskov08a: Peskov K, Goryanin I, Demin O (2008). "Kinetic model of phosphofructokinase-1 from Escherichia coli." J Bioinform Comput Biol 6(4);843-67. PMID: 18763746

Pham01: Pham AS, Janiak-Spens F, Reinhart GD (2001). "Persistent binding of MgADP to the E187A mutant of Escherichia coli phosphofructokinase in the absence of allosteric effects." Biochemistry 40(13);4140-9. PMID: 11300795

Pham01a: Pham AS, Reinhart GD (2001). "Pre-steady state quantification of the allosteric influence of Escherichia coli phosphofructokinase." J Biol Chem 276(37);34388-95. PMID: 11443117

Pham01b: Pham AS, Reinhart GD (2001). "MgATP-dependent activation by phosphoenolpyruvate of the E187A mutant of Escherichia coli phosphofructokinase." Biochemistry 40(13);4150-8. PMID: 11300796

Pham03: Pham AS, Reinhart GD (2003). "Quantification of allosteric influence of Escherichia coli phosphofructokinase by frequency domain fluorescence." Biophys J 85(1);656-66. PMID: 12829519

Reed03: Reed JL, Vo TD, Schilling CH, Palsson BO (2003). "An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR)." Genome Biol 4(9);R54. PMID: 12952533

Roehl76: Roehl RA, Vinopal RT (1976). "Lack of glucose phosphotransferase function in phosphofructokinase mutants of Escherichia coli." J Bacteriol 126(2);852-60. PMID: 177406

Rypniewski89: Rypniewski WR, Evans PR (1989). "Crystal structure of unliganded phosphofructokinase from Escherichia coli." J Mol Biol 1989;207(4);805-21. PMID: 2527305

Serre90: Serre MC, Garel JR (1990). "Role of the C-terminal region in the allosteric properties of Escherichia coli phosphofructokinase-1." Eur J Biochem 1990;189(3);487-92. PMID: 2140983

Shirakihara88: Shirakihara Y, Evans PR (1988). "Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products." J Mol Biol 1988;204(4);973-94. PMID: 2975709

Siedler12: Siedler S, Bringer S, Blank LM, Bott M (2012). "Engineering yield and rate of reductive biotransformation in Escherichia coli by partial cyclization of the pentose phosphate pathway and PTS-independent glucose transport." Appl Microbiol Biotechnol 93(4);1459-67. PMID: 22002070

Siedler14: Siedler S, Bringer S, Polen T, Bott M (2014). "NADPH-dependent reductive biotransformation with Escherichia coli and its pfkA deletion mutant: influence on global gene expression and role of oxygen supply." Biotechnol Bioeng 111(10);2067-75. PMID: 24771245

Thomas72: Thomas AD, Doelle HW, Westwood AW, Gordon GL (1972). "Effect of oxygen on several enzymes involved in the aerobic and anaerobic utilization of glucose in Escherichia coli." J Bacteriol 112(3);1099-105. PMID: 4344916

Tie12: Tie C, Reinhart GD (2012). "An in vivo approach to isolating allosteric pathways using hybrid multimeric proteins." Methods Mol Biol 796;307-15. PMID: 22052497

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

UniProt14: UniProt Consortium (2014). "UniProt version 2014-08 released on 2014-08-01 00:00:00." Database.

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

Vinopal75: Vinopal RT, Clifton D, Fraenkel DG (1975). "PfkA locus of Escherichia coli." J Bacteriol 122(3);1162-71. PMID: 125265

Wang01: Wang X, Kemp RG (2001). "Reaction path of phosphofructo-1-kinase is altered by mutagenesis and alternative substrates." Biochemistry 40(13);3938-42. PMID: 11300773

Wang13: Wang Y, San KY, Bennett GN (2013). "Improvement of NADPH bioavailability in Escherichia coli through the use of phosphofructokinase deficient strains." Appl Microbiol Biotechnol 97(15);6883-93. PMID: 23558585

Wang98a: Wang X, Deng Z, Kemp RG (1998). "An essential methionine residue involved in substrate binding by phosphofructokinases." Biochem Biophys Res Commun 250(2);466-8. PMID: 9753654

Wang99: Wang X, Kemp RG (1999). "Identification of residues of Escherichia coli phosphofructokinase that contribute to nucleotide binding and specificity." Biochemistry 38(14);4313-8. PMID: 10194349

Xia15: Xia T, Han Q, Costanzo WV, Zhu Y, Urbauer JL, Eiteman MA (2015). "Accumulation of d-Glucose from Pentoses by Metabolically Engineered Escherichia coli." Appl Environ Microbiol 81(10);3387-94. PMID: 25746993

Zheng92a: Zheng RL, Kemp RG (1992). "The mechanism of ATP inhibition of wild type and mutant phosphofructo-1-kinase from Escherichia coli." J Biol Chem 267(33);23640-5. PMID: 1429704

Zheng94: Zheng RL, Kemp RG (1994). "Identification of interactions that stabilize the transition state in Escherichia coli phosphofructo-1-kinase." J Biol Chem 269(28);18475-9. PMID: 8034595

Zheng94a: Zheng RL, Kemp RG (1994). "Site-directed mutagenesis of two highly conserved residues near the active site of phosphofructo-1-kinase." Biochem Biophys Res Commun 199(2);577-81. PMID: 8135798

Zheng95: Zheng RL, Kemp RG (1995). "Phosphofructo-1-kinase: role of charge neutralization in the active site." Biochem Biophys Res Commun 214(3);765-70. PMID: 7575542

Other References Related to Gene Regulation

Crooke95: Crooke H, Cole J (1995). "The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain." Mol Microbiol 1995;15(6);1139-50. PMID: 7623667

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

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

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

Negre96: Negre D, Bonod-Bidaud C, Geourjon C, Deleage G, Cozzone AJ, Cortay JC (1996). "Definition of a consensus DNA-binding site for the Escherichia coli pleiotropic regulatory protein, FruR." Mol Microbiol 1996;21(2);257-66. PMID: 8858581

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
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