Ontology highlight
ABSTRACT:
SUBMITTER: Lin G
PROVIDER: S-EPMC2930046 | biostudies-literature | 2010 Sep
REPOSITORIES: biostudies-literature
Lin Gang G Li Dongyang D Chidawanyika Tamutenda T Nathan Carl C Li Huilin H
Archives of biochemistry and biophysics 20100615 2
Via high-throughput screening of a natural compound library, we have identified a lipopeptide aldehyde, fellutamide B (1), as the most potent inhibitor of the Mycobacterium tuberculosis (Mtb) proteasome tested to date. Kinetic studies reveal that 1 inhibits both Mtb and human proteasomes in a time-dependent manner under steady-state condition. Remarkably, 1 inhibits the Mtb proteasome in a single-step binding mechanism with K(i)=6.8 nM, whereas it inhibits the human proteasome beta5 active site ...[more]