Unraveling Binding Mechanism and Stability of Urease Inhibitors: A QM/MM MD Study.

ABSTRACT: Soil bacteria can produce urease, which catalyzes the hydrolysis of urea to ammonia (NH₃) and carbamate. A variety of urease inhibitors have been proposed to reduce NH₃ volatilization by interfering with the urease activity. We report a quantum mechanics/molecular mechanics molecular dynamics (QM/MM MD) study on the mechanism employed for the inhibition of urease by three representative competitive inhibitors; namely, acetohydroxamic acid (AHA), hydroxyurea (HU), and N-(n-butyl)phosphorictriamide (NBPTO). The possible connections between the structural and thermodynamical properties and the experimentally observed inhibition efficiency were evaluated and characterized. We demonstrate that the binding affinity decreases in the order NBPTO >> AHA > HU in t

SUBMITTER: Suenaga S 

PROVIDER: S-EPMC10051795 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature