Structure and inhibition of diaminopimelic acid epimerase by slow-binding α-methyl amino acids.

ABSTRACT: Cofactor-independent racemases and epimerases produce D-amino acids from their L-isomers for a variety of biological processes. These enzymes operate via an unusual mechanism that relies on an active site cysteine thiolate (pK_a ~ 8.5) to deprotonate an amino acid α-carbon (pK_a ~ 29) and are of interest not only because of their biocatalytic potential for D-amino acid production, but also because many play key roles in biology and are antibiotic targets. However, obtaining crystal structures of these enzymes, especially in their closed, substrate- or inhibitor-bound conformations, is difficult. In this work, we characterized diaminopimelic acid (DAP) epimerase from the cyanobacterium Anabaena. DAP epimerase has long been of interest as an antibiotic target as it conver

SUBMITTER: Lamer T 

PROVIDER: S-EPMC12039745 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature