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Literature summary extracted from

  • Schneider, S.; Sandalova, T.; Schneider, G.; Sprenger, G.A.; Samland, A.K.
    Replacement of a phenylalanine by a tyrosine in the active site confers fructose 6-phosphate aldolase activity to the transaldolase of Escherichia coli and human origin (2008), J. Biol. Chem., 283, 30064-30072.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.2 mutant and wild-type protein are expressed in Escherichia coli as a GST-fusion protein Homo sapiens
2.2.1.2 mutant and wild-type protein are expressed in Escherichia coli as a His-tagged fusion protein Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.2.1.2 structure of the unliganded F178Y mutant is determined to 1.4 A resolution Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.2 F178Y by screening of library of proteins bearing a mutation in the active site mutant protein F178Y is found to be able to synthesize fructose 6-phosphate from dihydroxyacetone and glyceraldehyde 3-phosphate. Mutant is not only able to transfer a dihydroxyacetone moiety from a ketose donor, fructose 6-phosphate, onto an aldehyde acceptor, erythrose 4-phosphate, but to use it as a substrate directly in an aldolase reaction. Mutant fructose 6-phosphate aldolase activity is increased considerably above 70fold compared to wild-type. Structural studies of the wild-type and mutant protein suggest that this is due to a different H-bond pattern in the active site leading to a destabilization of the Schiff base intermediate Escherichia coli
2.2.1.2 F178Y reaction fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM): 30 (dihydroxyacetone), kcat (1/sec): 4.3 (dihydroxyacetone). Reaction fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM) 1.5 (fructose 6-phosphate), kcat (1/sec): 0.22 (fructose 6-phosphate). Reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate: Km (mM): 22 (fructose 6-phosphate), kcat (1/sec): 8.8 Escherichia coli
2.2.1.2 F189Y homologous human mutant F189 shows the same altered activity as mutant F179Y from Escherichia coli: mutant F189Y is able to synthesize fructose 6-phosphate from dihydroxyacetone and glyceraldehyde 3-phosphate. Mutant is not only able to transfer a dihydroxyacetone moiety from a ketose donor, fructose 6-phosphate, onto an aldehyde acceptor, erythrose 4-phosphate, but to use it as a substrate directly in an aldolase reaction Homo sapiens
2.2.1.2 F189Y reaction fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM): 340 (dihydroxyacetone), kcat (1/sec): 8.9 (dihydroxyacetone). Reaction fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM) 0.76 (fructose 6-phosphate), kcat (1/sec): 0.21 (fructose 6-phosphate). Reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate: Km (mM): 27 (fructose 6-phosphate), kcat (1/sec): 7.4 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.2 0.76
-
 D-fructose 6-phosphate mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate Homo sapiens
2.2.1.2 1.5
-
 D-fructose 6-phosphate mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate Escherichia coli
2.2.1.2 22
-
 D-fructose 6-phosphate mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate Escherichia coli
2.2.1.2 27
-
 D-fructose 6-phosphate mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate Homo sapiens
2.2.1.2 30
-
 dihydroxyacetone mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate Escherichia coli
2.2.1.2 340
-
 dihydroxyacetone mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.2.1.2 75000
-
 gel filtration Escherichia coli
2.2.1.2 77000
-
 gel filtration Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.2 Escherichia coli P0A870
-
-
2.2.1.2 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.2.1.2 affinity chromatography Homo sapiens
2.2.1.2 using Ni-NTA chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.2 dihydroxyacetone + D-glyceraldehyde 3-phosphate
-
 Homo sapiens D-fructose 6-phosphate
-
 ?
2.2.1.2 dihydroxyacetone + D-glyceraldehyde 3-phosphate
-
 Escherichia coli D-fructose 6-phosphate
-
 ?
2.2.1.2 sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 Homo sapiens D-erythrose 4-phosphate + D-fructose 6-phosphate
-
 ?
2.2.1.2 sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 Escherichia coli D-erythrose 4-phosphate + D-fructose 6-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.2.1.2 dimer gel filtration Homo sapiens
2.2.1.2 dimer gel filtration Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.2.1.2 hTAL
-
 Homo sapiens
2.2.1.2 TALB
-
 Escherichia coli
2.2.1.2 TALDO1
-
 Homo sapiens
2.2.1.2 transaldolase
-
 Escherichia coli
2.2.1.2 transaldolase1
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.2.1.2 30
-
 assay at Homo sapiens
2.2.1.2 30
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2.1.2 0.21
-
 D-fructose 6-phosphate mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate Homo sapiens
2.2.1.2 0.22
-
 D-fructose 6-phosphate mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate Escherichia coli
2.2.1.2 4.3
-
 dihydroxyacetone mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate Escherichia coli
2.2.1.2 7.4
-
 D-fructose 6-phosphate mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate Homo sapiens
2.2.1.2 8.8
-
 D-fructose 6-phosphate mutant F189Y, reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate Escherichia coli
2.2.1.2 8.9
-
 dihydroxyacetone mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.2.1.2 8.5
-
 assay at Homo sapiens
2.2.1.2 8.5
-
 assay at Escherichia coli