Structural highlights
Function[Q63SB3_BURPS] Removes the phosphate from trehalose 6-phosphate to produce free trehalose.[RuleBase:RU361117] Publication Abstract from PubMedWe report the functional and structural characterization of trehalose-6-phosphate phosphatase (TPP), from the Gram-negative bacterium B. pseudomallei that causes melioidosis, a severe infectious disease endemic in Southeast Asia and Northern Australia. TPP is a key enzyme in the trehalose biosynthesis pathway, which plays an important role in bacterial stress responses. Due to the absence of this biosynthetic pathway in mammals, TPP has drawn attention as a potential drug target, to combat antibiotic resistance. In this context, we present a detailed biochemical analysis of purified recombinant TPP, reporting its specific high catalytic activity toward the trehalose-6-phosphate substrate, and an absolute requirement for its Mg(2+) cofactor. Furthermore, we present the crystal structure of TPP solved at 1.74 A, revealing the canonical haloacid dehalogenase (HAD) superfamily fold and conserved substrate binding pocket, from which insights into the catalytic mechanism may be deduced. Our data represent a starting point for the rational design of antibacterial drugs. Functional and structural analysis of trehalose-6-phosphate phosphatase from Burkholderia pseudomallei: Insights into the catalytic mechanism.,Suthisawat S, Gourlay LJ, Bolognesi M, Boonyuen U, Vanaporn M Biochem Biophys Res Commun. 2020 Jan 20. pii: S0006-291X(20)30018-8. doi:, 10.1016/j.bbrc.2019.12.088. PMID:31973820[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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