Endonuclease V (ENDOV)

Endonuclease V (ENDOV) is a highly conserved endonuclease enzyme present from bacteria to humans. In prokaryotes, Endonuclease V acts mainly as a DNA repair enzyme, detecting and cleaving DNA at sites containing deaminated adenine (hypoxanthine) caused by nitrosative deamination. This activity is important for maintaining genomic integrity and preventing mutations that could lead to cancer[1][3]. Prokaryotic Endonuclease V recognizes damaged bases and makes an endonucleolytic cut one nucleotide downstream (3′) of the lesion site, a unique feature for DNA repair enzymes[1][4]. In contrast, in eukaryotes (including humans, where it is also known as hEndoV), the enzyme acts primarily on RNA, catalyzing the cleavage of single-stranded RNA at the 3′ position to inosine, which is a product of RNA editing or damage[2][3]. Human Endonuclease V localizes mostly to the cytoplasm and relocalizes to stress granules under cellular stress, suggesting a regulatory role in RNA metabolism and stress response, possibly linked to translation control and post-transcriptional regulation[2]. The gene encoding this enzyme in humans is ENDOV. There are no currently known drugs directly targeting Endonuclease V, nor is it a well-established biomarker or associated with particular safety concerns as a drug target. Its broader disease relevance—beyond mutagenesis and theoretical cancer risk—is not fully elucidated.

Other names

Endonuclease VENDOVhEndoVFLJ35220Inosine-specific endoribonucleaseinosine-specific endoribonuclease