ArticleScientific reports2017
Enzyme characteristics of pathogen-specific trehalose-6-phosphate phosphatases.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Polymorphism-driven transcriptomic changes in anthelmintic metabolism pathways of Anisakis simplex s.s. L3 larvae.Parasites & vectors · 2025Article
- Article
- Trehalose and bacterial virulence.Virulence · 2020Review
- A suicide inhibitor of nematode trehalose-6-phosphate phosphatases.Scientific reports · 2019Article
- DRfit: a Java tool for the analysis of discrete data from multi-well plate assays.BMC bioinformatics · 2019Article
- Infective larvae ofBiology open · 2019Article
- Synthesis and in Vitro Characterization of Trehalose-Based Inhibitors of Mycobacterial Trehalose 6-Phosphate Phosphatases.Chembiochem : a European journal of chemical biology · 2019Article
- Gene expression related to trehalose metabolism and its effect on Volvariella volvacea under low temperature stress.Scientific reports · 2018Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Owing to the key role of trehalose in pathogenic organisms, there has recently been growing interest in trehalose metabolism for therapeutic purposes. Trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB). Here, we compare the enzyme characteristics of recombinant TPPs from five important nematode and bacterial pathogens, including three novel members of this protein family. Analysis of the kinetics of trehalose-6-phosphate hydrolysis reveals that all five enzymes display a burst-like kinetic behaviour which is characterised by a decrease of the enzymatic rate after the pre-steady state. The observed super-stoichiometric burst amplitudes can be explained by multiple global conformational changes in members of this enzyme family during substrate processing. In the search for specific TPP inhibitors, the trapping of the complex conformational transitions in TPPs during the catalytic cycle may present a worthwhile strategy to explore.
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