Current methods and applications in the study of 1-Deoxy-D-xylulose 5-phosphate synthase (DXPS).

Authors

Victor O Gawriljuk, Siyao C Chen, Lydia J Kramer, Noah D Smith, Eleonora Diamanti, Anna K H Hirsch, Caren L Freel Meyers, Matthew R Groves

Published in

Methods in enzymology. Volume 736. Pages 61-94. Epub Sep 17, 2026.

Abstract

1-Deoxy-d-xylulose 5-phosphate synthase (DXPS, DXS, or DOXP synthase) catalyzes the formation of DXP in the first and rate-limiting step of the methylerythritol phosphate (MEP) pathway, essential for isoprenoid precursor biosynthesis in bacteria, plant plastids, and apicomplexan parasites. Its absence in humans makes DXPS an attractive target for antimicrobial and herbicide drug development, while its substrate and catalytic promiscuity and other structural and mechanistic features hints at potential multifunctionality in bacteria, and opens space for its use as a biocatalyst. In this chapter, we provide a concise overview of DXPS, including inhibition strategies, while highlighting key methodologies that enable its study. Approaches for recombinant expression and purification are discussed alongside techniques for structural elucidation. We further outline current strategies for inhibitor discovery and functional probe development, including biochemical and computational screening methods. The enzyme substrate and catalytic promiscuity is also addressed, emphasizing both the methods used to explore substrate and reaction scope, and implications for DXPS function in bacteria and its potential as a biocatalyst.

PMID:
42805709
Bibliographic data and abstract were imported from PubMed on 29 Sep 2026.

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