ArticleThe Journal of biological chemistry2008
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.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 61 citations in OpenAlex.
- Review
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- Decoding the Cell Atlas and Inflammatory Features of Human Intracranial Aneurysm Wall by Single-Cell RNA Sequencing.Journal of the American Heart Association · 2024Article
- The Impact of Viral Infection on the Chemistries of the Earth's Most Abundant Photosynthesizes: Metabolically Talented Aquatic Cyanobacteria.Biomolecules · 2023Article
- Characterization of an Entner-Doudoroff pathway-activated Escherichia coli.Biotechnology for biofuels and bioproducts · 2022Article
- Transaldolase in Bacillus methanolicus: biochemical characterization and biological role in ribulose monophosphate cycle.BMC microbiology · 2020Article
- Glycylglycine plays critical roles in the proliferation of spermatogonial stem cells.Molecular medicine reports · 2019Article
- Engineering aldolases as biocatalysts.Current opinion in chemical biology · 2014Review
- DHAP-dependent aldolases from (hyper)thermophiles: biochemistry and applications.Extremophiles : life under extreme conditions · 2014Review
- Improving upon nature: active site remodeling produces highly efficient aldolase activity toward hydrophobic electrophilic substrates.Biochemistry · 2012Article
- Computational tools for rational protein engineering of aldolases.Computational and structural biotechnology journal · 2012Review
- Phage auxiliary metabolic genes and the redirection of cyanobacterial host carbon metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism.Nature chemical biology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Based on a structure-assisted sequence alignment we designed 11 focused libraries at residues in the active site of transaldolase B from Escherichia coli and screened them for their ability to synthesize fructose 6-phosphate from dihydroxyacetone and glyceraldehyde 3-phosphate using a newly developed color assay. We found one positive variant exhibiting a replacement of Phe(178) to Tyr. This mutant variant is able not only to transfer a dihydroxyacetone moiety from a ketose donor, fructose 6-phosphate, onto an aldehyde acceptor, erythrose 4-phosphate (14 units/mg), but to use it as a substrate directly in an aldolase reaction (7 units/mg). With a single amino acid replacement the fructose-6-phosphate aldolase activity was increased considerably (>70-fold compared with 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. Furthermore, we show that a homologous replacement has a similar effect in the human transaldolase Taldo1 (aldolase activity, 14 units/mg). We also demonstrate that both enzymes TalB and Taldo1 are recognized by the same polyclonal antibody.
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