Jurgen Brem

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Biochemical and crystallographic studies of l,d-transpeptidase 2 from Mycobacterium tuberculosis with its natural monomer substrate - Communications Biology

Sep 17, 2024 | nature.com | Mariska de Munnik |Pauline A. Lang |Patrick Rabe |Jurgen Brem

AbstractThe essential l,d-transpeptidase of Mycobacterium tuberculosis (LdtMt2) catalyses the formation of 3\(\to\)3 cross-links in cell wall peptidoglycan and is a target for development of antituberculosis therapeutics. Efforts to inhibit LdtMt2 have been hampered by lack of knowledge of how it binds its substrate.

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