N-acylamino acid racemase (NAAAR)

N-acylamino acid racemase (NAAAR) is a member of the enolase superfamily that catalyzes the reversible racemization of various N-acylamino acids, converting between L- and D-enantiomers. Primarily identified in bacteria such as Amycolatopsis and Pseudomonas, this enzyme is divalent metal ion-dependent, typically requiring magnesium or manganese for catalytic activity. While NAAAR is most widely recognized for its utility in biocatalysis for the industrial production of optically pure L- or D-amino acids, it represents a potential target for antimicrobial strategies due to its role in specialized bacterial metabolism. In a therapeutic context, targeting NAAAR may disrupt the synthesis of essential peptidoglycan components or non-proteinogenic amino acids required for bacterial survival or virulence. Currently, there are no FDA-approved drugs specifically targeting this enzyme, though research into small-molecule inhibitors for metabolic study and anti-infective development is ongoing.

Other names

N-acyl-amino-acid racemaseN-acylamino-acid racemaseNAAAREC 5.1.1.10

Inhibition of bacterial cell wall component synthesis or interference with specialized metabolic pathways for non-canonical amino acids.