The structure of the monobactam-producing thioesterase domain of SulM forms a unique complex with the upstream carrier protein domain.

ABSTRACT: Nonribosomal peptide synthetases (NRPSs) are responsible for the production of important biologically active peptides. The large, multidomain NRPSs operate through an assembly line strategy in which the growing peptide is tethered to carrier domains that deliver the intermediates to neighboring catalytic domains. While most NRPS domains catalyze standard chemistry of amino acid activation, peptide bond formation, and product release, some canonical NRPS catalytic domains promote unexpected chemistry. The paradigm monobactam antibiotic sulfazecin is produced through the activity of a terminal thioesterase domain of SulM, which catalyzes an unusual β-lactam-forming reaction in which the nitrogen of the C-terminal N-sulfo-2,3-diaminopropionate residue attacks its thioester tether to release t

SUBMITTER: Patel KD 

PROVIDER: S-EPMC11298585 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature