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Updated: May 11, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Trehalases: a neglected carbon metabolism regulator?
Aarón Barraza1, Federico Sánchez
1Departamento de Biología Molecular de Plantas; Instituto de Biotecnología/Universidad Nacional Autónoma de México; Cuernavaca, Morelos, México.
Trehalase enzymes, crucial for breaking down trehalose, likely originated in bacteria, not eukaryotes. Their conserved structures across diverse organisms highlight important roles in metabolism and cellular regulation.
Area of Science:
- Enzymology
- Evolutionary Biology
- Biochemistry
Background:
- Trehalases catalyze the hydrolysis of trehalose, a non-reducing disaccharide.
- Previous hypotheses suggested an eukaryotic origin for trehalases.
- Trehalase enzymes are found across bacterial, plant, animal, and fungal lineages.
Purpose of the Study:
- To investigate the evolutionary origin of trehalases.
- To analyze the structural conservation and phylogenetic relationships of trehalases.
- To elucidate the diverse regulatory functions of trehalases.
Main Methods:
- Phylogenetic analysis of trehalase sequences.
- Comparative structural analysis of deduced and crystallographic trehalase structures.
- Identification of conserved motifs within trehalase structures.
Main Results:
- Trehalase phylogeny revealed three distinct branches: bacterial, plant/animal, and fungal.
- Enzyme structures are highly conserved despite sequence variations, suggesting a bacterial origin.
- Six conserved motifs were identified, indicating evolutionary selection for structural stability.
Conclusions:
- Trehalases likely possess a prokaryotic origin.
- These enzymes play significant roles in carbon metabolism.
- Trehalases are involved in various regulatory functions, including pathogen response, symbiosis, and energy supply.
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