Structural insights into stereochemical inversion by diaminopimelate epimerase: an antibacterial drug target.

ABSTRACT: D-amino acids are much less common than their L-isomers but are widely distributed in most organisms. Many D-amino acids, including those necessary for bacterial cell wall formation, are synthesized from the corresponding L-isomers by alpha-amino acid racemases. The important class of pyridoxal phosphate-independent racemases function by an unusual mechanism whose details have been poorly understood. It has been proposed that the stereoinversion involves two active-site cysteine residues acting in concert as a base (thiolate) and an acid (thiol). Although crystallographic structures of several such enzymes are available, with the exception of the recent structures of glutamate racemase from Bacillus subtilis and of proline racemase from Trypanosoma cruzi, the structures either are of inact

SUBMITTER: Pillai B 

PROVIDER: S-EPMC1482637 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature