|Gene:||fbaB||Accession Numbers: G7129 (EcoCyc), b2097, ECK2090|
Subunit composition of
fructose bisphosphate aldolase class I = [FbaB]10
fructose bisphosphate aldolase monomer = FbaB
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].
In earlier work it was thought that the Class I E. coli aldolase was a tetramer [Stribling73]|, but later studies showed that it is a decamer with an apparent molecular mass of 340,000 [Baldwin78a, Thomson98].
The E. coli Class I enzyme has been cloned, overexpressed and characterized. It shows low amino acid sequence identity with other Class I and Class II FBP aldolases from prokaryotes or eukaryotes. In the active site Lys236 was identified as the Schiff-base forming residue, and Lys238 is implicated in substrate binding [Thomson98].
Locations: cytosol, membrane
|Map Position: [2,175,534 <- 2,176,586] (46.89 centisomes, 169°)||Length: 1053 bp / 350 aa|
Molecular Weight of Polypeptide: 38.109 kD (from nucleotide sequence), 36.0 kD (experimental) [Thomson98]
Molecular Weight of Multimer: 340.0 kD (experimental) [Thomson98]
Unification Links: ASAP:ABE-0006941, DIP:DIP-36197N, EchoBASE:EB3815, EcoGene:EG14062, EcoliWiki:b2097, ModBase:P0A991, OU-Microarray:b2097, PortEco:fbaB, PR:PRO_000022575, Pride:P0A991, Protein Model Portal:P0A991, RefSeq:NP_416600, RegulonDB:G7129, SMR:P0A991, String:511145.b2097, UniProt:P0A991
|MultiFun Terms:||metabolism → energy metabolism, carbon → glycolysis|
|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
Comment 2] |
Yes [Feist07, Comment 4]
Enzymatic reaction of: fructose bisphosphate aldolase
EC Number: 18.104.22.168fructose 1,6-bisphosphate ⇄ glycerone phosphate + D-glyceraldehyde 3-phosphate
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
This reaction is reversible. [Thomson98]Alternative Substrates for fructose 1,6-bisphosphate: D-fructose 1-phosphate [Baldwin78a]
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)
Reduction by borohydride in the presence of fructose 1,6-bisphosphate or dihydroxyacetone phosphate irreversibly inhibits the enzyme. EDTA is not a inhibitor. Activation by several compounds tested was strongly pH-dependent. Fructose 1-phosphate is slowly cleaved and is not affected by activator compounds [Baldwin78a]]|.
|Substrate||Km (μM)||kcat (sec-1)||kcat/Km (sec-1 μM-1)||Citations|
|Chain||2 -> 350|
|Pfam PF01791||69 -> 326|
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.
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
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
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
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
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
Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371
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
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
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
Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293
Rodina11: Rodina E, Vorobieva N, Kurilova S, Mikulovich J, Vainonen J, Aro EM, Nazarova T (2011). "Identification of new protein complexes of Escherichia coli inorganic pyrophosphatase using pull-down assay." Biochimie 93(9);1576-83. PMID: 21664227
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
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
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
Lacour04: Lacour S, Landini P (2004). "SigmaS-dependent gene expression at the onset of stationary phase in Escherichia coli: function of sigmaS-dependent genes and identification of their promoter sequences." J Bacteriol 186(21);7186-95. PMID: 15489429
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