<i>De novo</i> cysteine biosynthesis in <i>Pseudomonas aeruginosa</i>: Characterization of the two main cysteine synthase isoforms.

ABSTRACT: Most bacteria synthesize L-cysteine via the reductive sulfate assimilation pathway, which is absent in humans and thus a promising source of antibiotic targets. Despite its relevance, this pathway remains poorly studied in Pseudomonas aeruginosa, a major antimicrobial resistance (AMR)-associated pathogen. We have identified the two main isoforms of cysteine synthase in P. aeruginosa (PA2709 and PA0932), which are pyridoxal 5'-phosphate-dependent enzymes that enable bacterial growth in minimal medium supplemented with either sulfate or thiosulfate. PA2709 is a classical O-acetylserine (OAS) sulfhydrylase, using bisulfide as a sulfur source. PA0932 also shows an OAS-dependent S-sulfocysteine synthase activity. Deletion of either one of the two genes does no

SUBMITTER: Martedi R 

PROVIDER: S-EPMC12800425 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature