Escherichia coli K-12 substr. MG1655 Enzyme: fructose bisphosphate aldolase class II

Gene: fbaA Accession Numbers: EG10282 (EcoCyc), b2925, ECK2921

Synonyms: ald, fba, fda

Regulation Summary Diagram: ?

Regulation summary diagram for fbaA

Subunit composition of fructose bisphosphate aldolase class II = [FbaA]2
         fructose bisphosphate aldolase monomer = FbaA

This enzyme catalyzes a reversible aldol cleavage/condensation reaction during glycolysis and gluconeogenesis in E. coli. In the glycolytic direction fructose 1,6-bisphosphate (FBP) is cleaved to produce glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (glycerone phosphate).

Two types of FBP aldolases have been distinguished, Class I and Class II. Class I FBP aldolases utilize an active site lysine residue to form a Schiff-base between the ε-amino group of lysine and the carbonyl group of the substrate. They also vary in subunit stoichiometry. Class II FBP aldolases are dimeric and utilize a divalent metal ion in catalysis via a similar mechanism. The Class I enzymes of eukaryotes have been well studied [Thomson98, Baldwin78, Baldwin78a, Stribling73, Alefounder89].

E. coli is one of a few organisms that expresses both classes of FBP aldolase [Stribling73, Baldwin78a]. The Class I enzyme encoded by fbaB is induced by gluconeogenic substrates, whereas the Class II enzyme encoded by fbaA is constitutive. When E. coli K-12 is grown on C-3 carbon sources both classes of aldolase are present, although the Class I enzyme is present only under these conditions. Therefore the Class I enzyme is most likely involved in gluconeogenesis and the Class II enzyme in glycolysis [Scamuffa80].

The E. coli enzyme resembles the typical class II aldolase from yeast in size and amino acid composition, strongly suggesting that they are related. These aldolases are found both in the eukaryotic green algae and fungi, and in the prokaryotic cyanobacteria and other bacteria [Baldwin78].

A number of studies provided initial characterizations of the enzyme including mutant phenotypes [Bock66, Bock66a, Schreyer73, Su75, Irani77], gene localization [Ruffler73, Alefounder89a], its metabolic regulation [Thomas72, Babul93], and evidence for its modification by phosphate [Babul88] and 2-mercaptoethanol [Packman95].

The enzyme has been cloned, overexpressed and purified in high yield [Henderson94]. Like other Class II enzymes, FbaA requires a divalent metal ion for activity. Zn2+ is isolated with the enzyme, but several other metal ions including Co2+, Fe2+ and Mn2+ can form an active metalloprotein complex [Scamuffa80]. His108 and His111 were identified as the zinc-binding ligands [Berry93]. The Arg331 residue is involved in substrate binding [Qamar96]. Asn286, Asp109 [Plater99], Asn35, Ser61, Lys325 [Zgiby00], and Glu182 [Zgiby02] also have roles in catalysis. A reaction mechanism has been proposed based on NMR spectroscopic data that involves an enzyme-bound enediol(ate) form of dihydroxyacetone phosphate as an intermediate [Szwergold95].

Following initial crystallization studies [Naismith92, Kitagawa95], crystal structures of the enzyme have been solved at 1.67 and 2.50 Å resolution [Blom96, Cooper96]. Crystal structures were also solved at 2.0 Å resolution in complex with phosphoglycolohydroxamate [Hall99], and with Cd2+ replacing Zn2+ at the active site [Hall03].

The ts8 and h8 mutations cause temperature-sensitive growth and inhibit stable RNA synthesis at the non-permissive temperature. Both mutations are located in the fbaA gene [Singer91, Singer91a]. The ts8 mutation was also shown to destabilize ptsG mRNA at the nonpermissive temperature [Morita03].

An fda mutant exhibits a heat-sensitive defect in rRNA transcription that is elicited via altered abundance of ppGpp and of initiating NTPs [Schneider03].

Directed evolution studies have resulted in fructose bisphosphate aldolase variants with increased temperature and organic solvent stability [Hao04]. The enzyme has also been engineered for increased activity toward N-Cbz-aminoaldehyde derivatives [Gutierrez11].

Competitive phosphoglycolosulfamate inhibitors of of the E. coli enzyme have been synthesized [Gavalda05]. Nickel toxicity in E. coli has been shown to be due to binding of nickel to the non-catalytic zinc site [Macomber11].

An NMR spectroscopy technique has been used for relaxation measurements of the E. coli enzyme [Burnley07].

A series of vectors inducibly expressing paired-terminus antisense RNAs was constructed to silence central carbon metabolism in host E. coli K-12 MG1655. A vector that silenced fbaA at 81% efficacy did not cause severe growth inhibition [Nakashima14].

Review: [Perham90]

Gene Citations: [Bardey05]

Locations: cytosol

Map Position: [3,068,187 <- 3,069,266] (66.13 centisomes, 238°)
Length: 1080 bp / 359 aa

Molecular Weight of Polypeptide: 39.147 kD (from nucleotide sequence), 40.0 kD (experimental) [Alefounder89 ]

Molecular Weight of Multimer: 78.0 kD (experimental) [Berry93]

Unification Links: ASAP:ABE-0009600 , CGSC:786 , DIP:DIP-31872N , EchoBASE:EB0278 , EcoGene:EG10282 , EcoliWiki:b2925 , OU-Microarray:b2925 , PortEco:fbaA , PR:PRO_000022574 , Pride:P0AB71 , Protein Model Portal:P0AB71 , RefSeq:NP_417400 , RegulonDB:EG10282 , SMR:P0AB71 , String:511145.b2925 , UniProt:P0AB71

Relationship Links: InterPro:IN-FAMILY:IPR000771 , InterPro:IN-FAMILY:IPR006411 , InterPro:IN-FAMILY:IPR013785 , PDB:Structure:1B57 , PDB:Structure:1DOS , PDB:Structure:1GYN , PDB:Structure:1ZEN , Pfam:IN-FAMILY:PF01116 , Prosite:IN-FAMILY:PS00602 , Prosite:IN-FAMILY:PS00806

In Paralogous Gene Group: 346 (4 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for fbaA

GO Terms:

Biological Process: GO:0006096 - glycolytic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11, GOA01a, Bock66]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0004332 - fructose-bisphosphate aldolase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Berry93, Scamuffa80, Bock66]
GO:0005515 - protein binding Inferred from experiment [Butland05]
GO:0008270 - zinc ion binding Inferred from experiment Inferred by computational analysis [GOA01a, Berry93, Katayama02]
GO:0042803 - protein homodimerization activity Inferred from experiment [Berry93]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11]
GO:0016832 - aldehyde-lyase activity Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ishihama08, LopezCampistrou05]

MultiFun Terms: metabolism carbon utilization carbon compounds

Essentiality data for fbaA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Last-Curated ? 06-Mar-2015 by Fulcher C , SRI International

Enzymatic reaction of: fructose bisphosphate aldolase

Synonyms: fructose-1,6-bisphosphate aldolase, fructose-1,6-bisphosphate triosephosphate lyase

EC Number:

fructose 1,6-bisphosphate <=> glycerone phosphate + D-glyceraldehyde 3-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.

This reaction is reversible. [Morse68]

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

The enzymes described in [Stribling73, Baldwin78] were purified from E. coli Crookes' strain.

Activation of the E. coli enzyme by NH4+ or K+ was cited in [Blom96] as a personal communication.

Cofactors or Prosthetic Groups: Zn2+ [Berry93, Scamuffa80]

Activators (Unknown Mechanism): K+ [Blom96] , ammonium [Blom96]

Inhibitors (Unknown Mechanism): Ni2+ [Macomber11] , EDTA [Stribling73]

Kinetic Parameters:

Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
fructose 1,6-bisphosphate

Enzymatic reaction of: sedoheptulose bisphosphate aldolase (fructose bisphosphate aldolase class II)

EC Number: 4.1.2.-

glycerone phosphate + D-erythrose 4-phosphate <=> D-sedoheptulose-1,7-bisphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the opposite direction.

In Pathways: sedoheptulose bisphosphate bypass

Sequence Features

Protein sequence of fructose bisphosphate aldolase monomer with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Alefounder89, Wilkins98, Link97, UniProt11]
UniProt: Removed.
Chain 2 -> 359
UniProt: Fructose-bisphosphate aldolase class 2;
N6-succinyllysine-Modification 9
[Zhang11, UniProt15]
UniProt: N6-succinyllysine; alternate.
N6-acetyllysine-Modification 9
[Peng11, Zhang09, UniProt15]
UniProt: N6-acetyllysine; alternate.
Mutagenesis-Variant 36
[Zgiby00, UniProt11]
UniProt: 1.5% of wild-type activity. 5-fold decrease in FBP affinity.
Mutagenesis-Variant 60
[Zgiby00, UniProt11]
UniProt: 81% of wild-type activity. 1.3-fold decrease in FBP affinity.
Mutagenesis-Variant 62
[Zgiby00, UniProt11]
[Zgiby00, UniProt11]
S → T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity.
S → A: 8% of wild-type activity. 16-fold decrease in FBP affinity.
Amino-Acid-Sites-That-Bind 62
UniProt: Glyceraldehyde 3-phosphate; Non-Experimental Qualifier: probable;
N6-succinyllysine-Modification 72
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Mutagenesis-Variant 108
[Berry93, UniProt11]
UniProt: Loss of activity.
Active-Site 110
[Hall99, UniProt11]
UniProt: Proton donor.
Metal-Binding-Site 111
[Hall99, Cooper96, Blom96, UniProt15]
UniProt: Zinc 1; catalytic.
Mutagenesis-Variant 111
[Berry93, UniProt11]
UniProt: Loss of activity.
Mutagenesis-Variant 112
[Berry93, UniProt11]
UniProt: Partial loss of activity.
N6-succinyllysine-Modification 115
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Metal-Binding-Site 145
[Hall99, Cooper96, Blom96, UniProt15]
UniProt: Zinc 2.
Metal-Binding-Site 175
[Hall99, Cooper96, Blom96, UniProt15]
UniProt: Zinc 2.
Metal-Binding-Site 227
[Hall99, Cooper96, Blom96, UniProt15]
UniProt: Zinc 1; catalytic.
Amino-Acid-Sites-That-Bind 228
UniProt: Dihydroxyacetone phosphate; via amide nitrogen.
N6-succinyllysine-Modification 231
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
N6-succinyllysine-Modification 251
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Metal-Binding-Site 265
[Hall99, Cooper96, Blom96, UniProt15]
UniProt: Zinc 1; catalytic.
Protein-Segment 266 -> 268
UniProt: Dihydroxyacetone phosphate binding; Sequence Annotation Type: region of interest;
Protein-Segment 287 -> 290
UniProt: Dihydroxyacetone phosphate binding; Sequence Annotation Type: region of interest;
N6-succinyllysine-Modification 319
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
N6-succinyllysine-Modification 326
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.
Mutagenesis-Variant 326
[Zgiby00, UniProt11]
UniProt: 6% of wild-type activity. 2.2-fold decrease in FBP affinity.
N6-succinyllysine-Modification 348
[Zhang11, UniProt12a]
UniProt: N6-succinyllysine.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b2925 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10282; confirmed by SwissProt match.


Alefounder89: Alefounder PR, Baldwin SA, Perham RN, Short NJ (1989). "Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli." Biochem J 1989;257(2);529-34. PMID: 2649077

Alefounder89a: Alefounder PR, Perham RN (1989). "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli." Mol Microbiol 3(6);723-32. PMID: 2546007

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

Babul88: Babul J, Fraenkel DG (1988). "Phosphate modification of fructose-1,6-bisphosphate aldolase in Escherichia coli." Biochem Biophys Res Commun 151(3);1033-8. PMID: 3281666

Babul93: Babul J, Clifton D, Kretschmer M, Fraenkel DG (1993). "Glucose metabolism in Escherichia coli and the effect of increased amount of aldolase." Biochemistry 32(17);4685-92. PMID: 8485146

Baldwin78: Baldwin SA, Perham RN, Stribling D (1978). "Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)." Biochem J 1978;169(3);633-41. PMID: 417719

Baldwin78a: Baldwin SA, Perham RN (1978). "Novel kinetic and structural properties of the class-I D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)." Biochem J 1978;169(3);643-52. PMID: 348198

Bardey05: Bardey V, Vallet C, Robas N, Charpentier B, Thouvenot B, Mougin A, Hajnsdorf E, Regnier P, Springer M, Branlant C (2005). "Characterization of the molecular mechanisms involved in the differential production of erythrose-4-phosphate dehydrogenase, 3-phosphoglycerate kinase and class II fructose-1,6-bisphosphate aldolase in Escherichia coli." Mol Microbiol 57(5);1265-87. PMID: 16102000

Berry93: Berry A, Marshall KE (1993). "Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli." FEBS Lett 318(1);11-6. PMID: 8436219

Blom96: Blom NS, Tetreault S, Coulombe R, Sygusch J (1996). "Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase." Nat Struct Biol 3(10);856-62. PMID: 8836102

Bock66: Bock A, Neidhardt FC (1966). "Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity." J Bacteriol 92(2);464-469. PMID: 16562136

Bock66a: Bock A, Neidhardt FC (1966). "Properties of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase." J Bacteriol 92(2);470-6. PMID: 16562137

Burnley07: Burnley BT, Kalverda AP, Paisey SJ, Berry A, Homans SW (2007). "Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins." J Biomol NMR 39(3);239-45. PMID: 17882509

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Cooper96: Cooper SJ, Leonard GA, McSweeney SM, Thompson AW, Naismith JH, Qamar S, Plater A, Berry A, Hunter WN (1996). "The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold." Structure 4(11);1303-15. PMID: 8939754

Gavalda05: Gavalda S, Braga R, Dax C, Vigroux A, Blonski C (2005). "N-Sulfonyl hydroxamate derivatives as inhibitors of class II fructose-1,6-diphosphate aldolase." Bioorg Med Chem Lett 15(24);5375-7. PMID: 16236509

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."

Gutierrez11: Gutierrez M, Parella T, Joglar J, Bujons J, Clapes P (2011). "Structure-guided redesign of D-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation." Chem Commun (Camb) 47(20);5762-4. PMID: 21499643

Hall03: Hall DR, Kemp LE, Leonard GA, Marshall K, Berry A, Hunter WN (2003). "The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase." Acta Crystallogr D Biol Crystallogr 59(Pt 3);611-4. PMID: 12595741

Hall99: Hall DR, Leonard GA, Reed CD, Watt CI, Berry A, Hunter WN (1999). "The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity." J Mol Biol 287(2);383-94. PMID: 10080900

Hao04: Hao J, Berry A (2004). "A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents." Protein Eng Des Sel 17(9);689-97. PMID: 15531627

Henderson94: Henderson I, Garcia-Junceda E, Liu KK, Chen YL, Shen GJ, Wong CH (1994). "Cloning, overexpression and isolation of the type II FDP aldolase from E. coli for specificity study and synthetic application." Bioorg Med Chem 2(8);837-43. PMID: 7894977

Irani77: Irani MH, Maitra PK (1977). "Properties of Escherichia coli mutants deficient in enzymes of glycolysis." J Bacteriol 132(2);398-410. PMID: 410789

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

Katayama02: Katayama A, Tsujii A, Wada A, Nishino T, Ishihama A (2002). "Systematic search for zinc-binding proteins in Escherichia coli." Eur J Biochem 269(9);2403-13. PMID: 11985624

Kitagawa95: Kitagawa Y, Leonard GA, Harrop SJ, Peterson MR, Hunter WN, Qamar S, Berry A (1995). "Additional crystal forms of the E. coli class II fructose-1,6-bisphosphate aldolase." Acta Crystallogr D Biol Crystallogr 51(Pt 5);833-4. PMID: 15299818

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

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

Macomber11: Macomber L, Elsey SP, Hausinger RP (2011). "Fructose-1,6-bisphosphate aldolase (class II) is the primary site of nickel toxicity in Escherichia coli." Mol Microbiol 82(5);1291-300. PMID: 22014167

Morita03: Morita T, El-Kazzaz W, Tanaka Y, Inada T, Aiba H (2003). "Accumulation of glucose 6-phosphate or fructose 6-phosphate is responsible for destabilization of glucose transporter mRNA in Escherichia coli." J Biol Chem 278(18);15608-14. PMID: 12578824

Morse68: Morse DE, Horecker BL (1968). "The mechanism of action of aldolases." Adv Enzymol Relat Areas Mol Biol 31;125-81. PMID: 4880215

Naismith92: Naismith JH, Ferrara JD, Bailey S, Marshall K, Dauter Z, Wilson KS, Habash J, Harrop SJ, Berry AJ, Hunter WN (1992). "Initiating a crystallographic study of a class II fructose-1,6-bisphosphate aldolase." J Mol Biol 225(4);1137-41. PMID: 1613797

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

Packman95: Packman LC, Berry A (1995). "A reactive, surface cysteine residue of the class-II fructose-1,6-bisphosphate aldolase of Escherichia coli revealed by electrospray ionisation mass spectrometry." Eur J Biochem 227(1-2);510-5. PMID: 7851430

Peng11: Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y (2011). "The first identification of lysine malonylation substrates and its regulatory enzyme." Mol Cell Proteomics 10(12);M111.012658. PMID: 21908771

Perham90: Perham RN (1990). "The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes." Biochem Soc Trans 18(2);185-7. PMID: 2199259

Plater99: Plater AR, Zgiby SM, Thomson GJ, Qamar S, Wharton CW, Berry A (1999). "Conserved residues in the mechanism of the E. coli Class II FBP-aldolase." J Mol Biol 285(2);843-55. PMID: 9878448

Qamar96: Qamar S, Marsh K, Berry A (1996). "Identification of arginine 331 as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli." Protein Sci 5(1);154-61. PMID: 8771208

Ruffler73: Ruffler D, Bock A (1973). "Location of the structural gene for fructose-1,6-diphosphate aldolase in Escherichia coli." J Bacteriol 116(2);1054-5. PMID: 4583229

Scamuffa80: Scamuffa MD, Caprioli RM (1980). "Comparison of the mechanisms of two distinct aldolases from Escherichia coli grown on gluconeogenic substrates." Biochim Biophys Acta 1980;614(2);583-90. PMID: 6996735

Schneider03: Schneider DA, Gourse RL (2003). "Changes in the concentrations of guanosine 5'-diphosphate 3'-diphosphate and the initiating nucleoside triphosphate account for inhibition of rRNA transcription in fructose-1,6-diphosphate aldolase (fda) mutants." J Bacteriol 185(20);6192-4. PMID: 14526031

Schreyer73: Schreyer R, Bock A (1973). "Phenotypic suppression of a fructose-1,6-diphosphate aldolase mutation in Escherichia coli." J Bacteriol 115(1);268-76. PMID: 4577744

Singer91: Singer M, Walter WA, Cali BM, Rouviere P, Liebke HH, Gourse RL, Gross CA (1991). "Physiological effects of the fructose-1,6-diphosphate aldolase ts8 mutation on stable RNA synthesis in Escherichia coli." J Bacteriol 173(19);6249-57. PMID: 1717436

Singer91a: Singer M, Rossmiessl P, Cali BM, Liebke H, Gross CA (1991). "The Escherichia coli ts8 mutation is an allele of fda, the gene encoding fructose-1,6-diphosphate aldolase." J Bacteriol 173(19);6242-8. PMID: 1917856

Stribling73: Stribling D, Perham RN (1973). "Purification and characterization of two fructose diphosphate aldolases from Escherichia coli (Crookes' strain)." Biochem J 1973;131(4);833-41. PMID: 4198624

Su75: Su CH, Merlie JP, Goldfine H (1975). "Rapid cessation of phospholipid synthesis in fructose-1,6-diphosphate aldolase mutants of Escherichia coli." J Bacteriol 122(2);565-9. PMID: 1092657

Szwergold95: Szwergold BS, Ugurbil K, Brown TR (1995). "Properties of fructose-1,6-bisphosphate aldolase from Escherichia coli: an NMR analysis." Arch Biochem Biophys 317(1);244-52. PMID: 7872790

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

Thomson98: Thomson GJ, Howlett GJ, Ashcroft AE, Berry A (1998). "The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase." Biochem J 1998;331 ( Pt 2);437-45. PMID: 9531482

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

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-09 released on 2012-09-12 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 manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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

Wilkins98: Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278(3);599-608. PMID: 9600841

Zgiby00: Zgiby SM, Thomson GJ, Qamar S, Berry A (2000). "Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases." Eur J Biochem 267(6);1858-68. PMID: 10712619

Zgiby02: Zgiby S, Plater AR, Bates MA, Thomson GJ, Berry A (2002). "A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli." J Mol Biol 315(2);131-40. PMID: 11779234

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

Zhang11: Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y (2011). "Identification of lysine succinylation as a new post-translational modification." Nat Chem Biol 7(1);58-63. PMID: 21151122

Other References Related to Gene Regulation

Charpentier98: Charpentier B, Bardey V, Robas N, Branlant C (1998). "The EIIGlc protein is involved in glucose-mediated activation of Escherichia coli gapA and gapB-pgk transcription." J Bacteriol 1998;180(24);6476-83. PMID: 9851989

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

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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