Aspergillomarasmine A inhibits metallo-β-lactamases by selectively sequestering Zn².

ABSTRACT: Class B metallo-β-lactamases (MBLs) are Zn²⁺-dependent enzymes that catalyze the hydrolysis of β-lactam antibiotics to confer resistance in bacteria. Several problematic groups of MBLs belong to subclass B1, including the binuclear New Delhi MBL (NDM), Verona integrin-encoded MBL, and imipenemase-type enzymes, which are responsible for widespread antibiotic resistance. Aspergillomarasmine A (AMA) is a natural aminopolycarboxylic acid that functions as an effective inhibitor of class B1 MBLs. The precise mechanism of action of AMA is not thoroughly understood, but it is known to inactivate MBLs by removing one catalytic Zn²⁺ cofactor. We investigated the kinetics of MBL inactivation in detail and report that AMA is a selective Zn²⁺ scavenger that indirectly

SUBMITTER: Sychantha D 

PROVIDER: S-EPMC8319579 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature