ArticleApplied and environmental microbiology2015
Identification of GH15 Family Thermophilic Archaeal Trehalases That Function within a Narrow Acidic-pH Range.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 29 citations in OpenAlex.
- Evolutionary Analysis of Trehalose Breakdown Pathways.Genome biology and evolution · 2026Article
- Aromatic residues in N-terminal domain of archaeal trehalase affect the folding and activity of catalytic domain.Applied microbiology and biotechnology · 2024Article
- Elucidation of bacterial trehalose-degrading trehalase and trehalose phosphorylase: physiological significance and its potential applications.Glycobiology · 2024Review
- Evolutionary patterns of archaea predominant in acidic environment.Environmental microbiome · 2023Article
- Evaluation of the roles of hydrophobic residues in the N-terminal region of archaeal trehalase in its folding.Applied microbiology and biotechnology · 2021Article
- Salt Stress Response of Sulfolobus acidocaldarius Involves Complex Trehalose Metabolism Utilizing a Novel Trehalose-6-Phosphate Synthase (TPS)/Trehalose-6-Phosphate Phosphatase (TPP) Pathway.Applied and environmental microbiology · 2020Article
- Acidic Chitinase-Chitin Complex Is Dissociated in a Competitive Manner by Acetic Acid: Purification of Natural Enzyme for Supplementation Purposes.International journal of molecular sciences · 2018Article
- Microbial Community Structure and Functional Potential Along a Hypersaline Gradient.Frontiers in microbiology · 2018Article
- Characterization of a Bacillus thuringiensis chitinase that binds to cellulose and chitin.AMB Express · 2017Article
- Two Novel Glycoside Hydrolases Responsible for the Catabolism of Cyclobis-(1→6)-α-nigerosyl.The Journal of biological chemistry · 2016Article
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8 authors at 1 institution in 1 country.
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Abstract
Two glucoamylase-like genes, TVN1315 and Ta0286, from the archaea Thermoplasma volcanium and T. acidophilum, respectively, were expressed in Escherichia coli. The gene products, TVN1315 and Ta0286, were identified as archaeal trehalases. These trehalases belong to the CAZy database family GH15, although they have putative (α/α)6 barrel catalytic domain structures similar to those of GH37 and GH65 family trehalases from other organisms. These newly identified trehalases function within a narrow range of acidic pH values (pH 3.2 to 4.0) and at high temperatures (50 to 60°C), and these enzymes display Km values for trehalose higher than those observed for typical trehalases. These enzymes were inhibited by validamycin A; however, the inhibition constants (Ki) were higher than those of other trehalases. Three TVN1315 mutants, corresponding to E408Q, E571Q, and E408Q/E571Q mutations, showed reduced activity, suggesting that these two glutamic acid residues are involved in trehalase catalysis in a manner similar to that of glucoamylase. To date, TVN1315 and Ta0286 are the first archaeal trehalases to be identified, and this is the first report of the heterologous expression of GH15 family trehalases. The identification of these trehalases could extend our understanding of the relationships between the structure and function of GH15 family enzymes as well as glycoside hydrolase family enzymes; additionally, these enzymes provide insight into archaeal trehalose metabolism.
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