Mammalian Nudt15 hydrolytic and binding activity on methylated guanosine mononucleotides.

ABSTRACT: The Nudt15 enzyme of the NUDIX protein family is the subject of extensive study due to its action on thiopurine drugs used in the treatment of cancer and inflammatory diseases. In addition to thiopurines, Nudt15 is enzymatically active in vitro on several nucleotide substrates. It has also been suggested that this enzyme may play a role in 5'RNA turnover by hydrolyzing m⁷GDP, a product of mRNA decapping. However, no detailed studies on this substrate with Nudt15 are available. Here, we analyzed the enzymatic activity of Nudt15 with m⁷GDP, its triphosphate form m⁷GTP, and the trimethylated counterparts (m₃^2,2,7GDP and m₃^2,2,7GTP). Kinetic data revealed a moderate activity of Nudt15 toward these methylated mononucle

SUBMITTER: Lukaszewicz M 

PROVIDER: S-EPMC10618335 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature