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Transaldolase: from biochemistry to human disease
Anne K Samland1, Georg A Sprenger
1The Institute of Microbiology, Universität Stuttgart, Allmandring 31, Stuttgart, Germany. anne.samland@imb.uni-stuttgart.de
The International Journal of Biochemistry & Cell Biology
|April 30, 2009
Summary
Transaldolase (TAL) is crucial for metabolism, transferring sugar groups. Its deficiency causes severe human disease, unlike in microbes, highlighting its vital role.
Area of Science:
- Biochemistry
- Metabolic pathways
- Enzymology
Background:
- Transaldolase (TAL) is a key enzyme in the pentose phosphate pathway.
- It catalyzes the transfer of dihydroxyacetone groups between sugar phosphates.
- TAL is essential for central metabolism and cellular function.
Purpose of the Study:
- To review the biochemical properties, structure, and function of transaldolase.
- To explore the evolutionary relationships and subfamilies of transaldolases.
- To discuss the implications of transaldolase deficiency in human diseases.
Main Methods:
- Phylogenetic analysis to distinguish transaldolase subfamilies.
- Three-dimensional structural determination of bacterial and human transaldolase.
- Mutagenesis studies to elucidate the reaction mechanism.
- Review of existing literature on transaldolase function and disease association.
Main Results:
- Five transaldolase subfamilies were identified, including those with known activity and related enzymes.
- The 3D structures of E. coli TAL B and human TALDO1 were solved, revealing structural insights.
- The reaction mechanism involves a cofactor-less Schiff base intermediate.
- While microbial TAL deficiency is tolerated, human deficiency leads to severe symptoms.
Conclusions:
- Transaldolase plays a critical, non-redundant role in human metabolism.
- Structural and mechanistic insights aid in understanding enzyme function.
- TAL deficiency is linked to severe human health conditions, including oxidative stress, apoptosis, multiple sclerosis, and cancer.
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