<i>S</i>-Adenosylmethionine-responsive cystathionine β-synthase modulates sulfur metabolism and redox balance in <i>Mycobacterium</i> <i>tuberculosis</i>.

ABSTRACT: Methionine and cysteine metabolisms are important for the survival and pathogenesis of Mycobacterium tuberculosis (Mtb). The transsulfuration pathway converts methionine to cysteine and represents an important link between antioxidant and methylation metabolism in diverse organisms. Using a combination of biochemistry and cryo-electron microscopy, we characterized the first enzyme of the transsulfuration pathway, cystathionine β-synthase (MtbCbs) in Mtb. We demonstrated that MtbCbs is a heme-less, pyridoxal-5'-phosphate-containing enzyme, allosterically activated by S-adenosylmethionine (SAM). The atomic model of MtbCbs in its native and SAM-bound conformations revealed a unique mode of SAM-dependent allosteric activation. Further, SAM stabi

SUBMITTER: Bandyopadhyay P 

PROVIDER: S-EPMC9232105 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature