A single Leishmania adenylate-forming enzyme of the ANL superfamily generates both acetyl- and acetoacetyl-CoA.

ABSTRACT: Leishmania, a protozoan parasite, is responsible for significant morbidity and mortality worldwide, manifesting as cutaneous, mucocutaneous, and visceral leishmaniasis. These diseases pose a substantial burden, especially in impoverished regions with limited access to effective medical treatments. Current therapies are toxic, have low efficacy, and face growing resistance. Understanding the metabolic pathways of Leishmania, particularly those differing from its host, can unveil potential therapeutic targets. In this study, we investigated the acetyl-CoA synthetase (ACS) enzyme from Leishmania infantum (LiAcs1), which, unlike many organisms, also exhibits acetoacetyl-CoA synthetase (KBC) activity. This dual functionality is unique among acyl-CoA/NRPS/luciferase superfamily enzymes and cruci

SUBMITTER: Jezewski AJ 

PROVIDER: S-EPMC11584562 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature