Novel Calcium-Binding Motif Stabilizes and Increases the Activity of Aspergillus fumigatus Ecto-NADase.

ABSTRACT: Nicotinamide adenine dinucleotide (NAD) is an essential molecule in all kingdoms of life, mediating energy metabolism and cellular signaling. Recently, a new class of highly active fungal surface NADases was discovered. The enzyme from the opportunistic human pathogen Aspergillus fumigatus was thoroughly characterized. It harbors a catalytic domain that resembles that of the tuberculosis necrotizing toxin from Mycobacterium tuberculosis, which efficiently cleaves NAD⁺ to nicotinamide and ADP-ribose, thereby depleting the dinucleotide pool. Of note, the A. fumigatus NADase has an additional Ca²⁺-binding motif at the C-terminus of the protein. Despite the presence of NADases in several fungal divisions, the Ca²⁺-binding motif is uniquely

SUBMITTER: Ferrario E 

PROVIDER: S-EPMC10666276 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature