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Target intelligence / Profile preview
L-allo-threonine aldolase (L-ATA)
- Target
- L-ATA
- Molecular classification
- Enzyme, Lyase, Aldolase, Pyridoxal phosphate-dependent enzyme
01
Overview
L-allo-threonine aldolase from the hyperthermophilic bacterium Thermotoga maritima is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible cleavage of L-allo-threonine into glycine and acetaldehyde (UniProt: Q9X1P6). This enzyme is highly valued in the field of biocatalysis due to its exceptional thermostability and its ability to synthesize various beta-hydroxy-alpha-amino acids through aldol addition (PubMed: 12460569). These amino acids serve as critical intermediates in the production of diverse pharmaceutical agents. However, this enzyme is not a therapeutic target for human diseases, nor is it found in human physiology. Its primary application remains in industrial biotechnology and green chemistry rather than clinical medicine. Consequently, there are no known interacting drugs, biomarkers, or disease roles associated with this specific bacterial protein.
- Other names
- L-allo-threonine acetaldehyde-lyaseTM0295Thermotoga maritima L-allo-threonine aldolase
02
Mechanism of action
Catalyzes the pyridoxal-5'-phosphate (PLP)-dependent reversible cleavage of L-allo-threonine into glycine and acetaldehyde (UniProt: Q9X1P6).
03
Biological functions
Amino acid metabolismBiocatalysisAldol cleavageSynthesis of beta-hydroxy-alpha-amino acids
04
Safety considerations
Potential immunogenicity if introduced into human systemsLack of relevance to human disease pathways
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