The biosynthesis of N-acyalated tryptazolone in Mycobacterium tuberculosis and related bacteria.

ABSTRACT: The ability of Mycobacterium tuberculosis (Mtb) to thrive within its host is due in part to its complex lipid metabolism, aspects of which remain poorly understood. We recently reported the production of N-acylated tyrazolones, a class of oxazolones, by the tyzACB gene cluster in Mtb. We now report that Mtb also produces N-acylated tryptazolones using a second biosynthetic cluster, trzAS. TrzA catalyzed the N-acylation of l-tryptophan with the highest specificity for C_5:0-CoA among acyl-CoAs (k_cat/K_m = 2.3 ± 0.3 × 10³ M^-1s^-1). Similarly, TrzS, comprising a ThiF-like cyclase fused to a flavin-dependent oxidase, catalyzed the ATP-dependent cyclization and O₂-dependent desaturation of the acylated amino acid to yield

SUBMITTER: Kleetz J 

PROVIDER: S-EPMC12856293 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature