Journal article

Enzyme characteristics of pathogen-specific trehalose-6-phosphate phosphatases

Megan Cross, Siji Rajan, Janine Chekaiban, Jake Saunders, Chloe Hamilton, Jeong-Sun Kim, Mark J Coster, Robin B Gasser, Andreas Hofmann



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 amplitud..

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Awarded by Chonnam National University

Funding Acknowledgements

Research in the investigators' laboratories is funded by the Australian Research Council, the National Health and Medical Research Council (A.H. and R.B.G.), the Rebecca L. Cooper Medical Research Foundation (A.H.) and Chonnam National University (2015-0597, J.S.K.). The Equity Trustees PhD Scholarship and Australian Government Research Training Program Scholarship (M.C.) is gratefully acknowledged. Mass spectrometric analysis was undertaken at the Australian Proteome Analysis Facility (APAF), the infrastructure provided by the Australian Government through the National Collaborative Research Infrastructure Strategy (NCRIS).