Any feedback?
Literature summary for 2.2.1.2 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| mutant and wild-type protein are expressed in Escherichia coli as a GST-fusion protein | Homo sapiens |
| mutant and wild-type protein are expressed in Escherichia coli as a His-tagged fusion protein | Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure of the unliganded F178Y mutant is determined to 1.4 A resolution | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.76 | - |
D-fructose 6-phosphate | mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate | Homo sapiens |  |
| 1.5 | - |
D-fructose 6-phosphate | mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate | Escherichia coli | |
| 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 | |
| 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 | |
| 30 | - |
dihydroxyacetone | mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate | Escherichia coli | |
| 340 | - |
dihydroxyacetone | mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate | Homo sapiens | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 75000 | - |
gel filtration | Escherichia coli |
| 77000 | - |
gel filtration | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A870 | - |
- |
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| affinity chromatography | Homo sapiens |
| using Ni-NTA chromatography | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dihydroxyacetone + D-glyceraldehyde 3-phosphate | - |
Homo sapiens | D-fructose 6-phosphate | - |
? | |
| dihydroxyacetone + D-glyceraldehyde 3-phosphate | - |
Escherichia coli | D-fructose 6-phosphate | - |
? | |
| sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate | - |
Homo sapiens | D-erythrose 4-phosphate + D-fructose 6-phosphate | - |
? | |
| sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate | - |
Escherichia coli | D-erythrose 4-phosphate + D-fructose 6-phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | gel filtration | Homo sapiens |
| dimer | gel filtration | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| hTAL | - |
Homo sapiens |
| TALB | - |
Escherichia coli |
| TALDO1 | - |
Homo sapiens |
| transaldolase | - |
Escherichia coli |
| transaldolase1 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Homo sapiens |
| 30 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.21 | - |
D-fructose 6-phosphate | mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate | Homo sapiens | |
| 0.22 | - |
D-fructose 6-phosphate | mutant F189Y, reaction: fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate | Escherichia coli | |
| 4.3 | - |
dihydroxyacetone | mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate | Escherichia coli | |
| 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 | |
| 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 | |
| 8.9 | - |
dihydroxyacetone | mutant F189Y, reaction: fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate | Homo sapiens | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Homo sapiens |
| 8.5 | - |
assay at | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
