Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases

Abstract

M. tuberculosis NAD+ synthetase (tbNadE) is of interest as a drug target. Here the authors present the actively trapped Homo sapiens NAD+ synthetase (hsNadE) and tbNadE structures and show key differences in the synthetase active site and in structural elements possibly involved in the allosteric regulation of catalysis to be leveraged for the development of M. tuberculosis selective inhibitors.