The Nitro Group as a Masked Electrophile in Covalent Enzyme Inhibition.

ABSTRACT: We report the unprecedented reaction between a nitroalkane and an active-site cysteine residue to yield a thiohydroximate adduct. Structural and kinetic evidence suggests the nitro group is activated by conversion to its nitronic acid tautomer within the active site. The nitro group, therefore, shows promise as a masked electrophile in the design of covalent inhibitors targeting binding pockets with appropriately placed cysteine and general acid residues.

SUBMITTER: Ray S 

PROVIDER: S-EPMC6300134 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature