Native mass spectrometry reveals DltA catalysis, DltC loading, and inhibition in the d -alanylation pathway

2026/01/01 by Yi Wang, Hannah Squires, Marian Aba Addo +5 · 1 voice
Biochemistry, Genetics and Molecular Biology · Materials Science · #Amino Acid Enzymes and Metabolism #Cancer, Hypoxia, and Metabolism #Enzyme Structure and Function

paper · doi:10.1039/d6ra04213a

openalex publication_date 2026/01/01 · openalex created_date 2026/06/03 · openalex updated_date 2026/07/27

Abstract

-DltC. This process was inhibited by a sulfamoyl-adenosine compound that mimics the adenylate intermediate. Mutational analysis of the conserved DltA P-loop revealed position-specific effects on catalysis, highlighting structural features that govern substrate processing. Together, these findings define regulatory steps in the Dlt pathway and identify opportunities for targeted inhibition. The same strategy should be adaptable to other systems in which transient acyl- or aminoacyl-carrier protein intermediates are difficult to monitor directly.

Discussions

• Check out this recent article by previous RSC president Carol Robinson, Jani Bolla and coworkers on monitoring the DltA-mediated activation of D-alanine and DltC carrier protein loading using mass spe [bsky, 0 points, 0 comments]

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