title: Inosine-specific ribonuclease activity of natural variants of human endonuclease V.
abstract: Adenine bases in DNA, RNA, and nucleotides are deaminated during normal metabolism via hydrolytic and nitrosative reactions. In RNA, the deaminated product inosine is resolved by human endonuclease V, and mice deficient in this enzyme are cancer-prone. We have now produced, purified, and characterized naturally occurring variants of human endonuclease V (V29I, R112Q, K114R, H141Y, and D201N). We found that H141Y, but not other variants, is catalytically impaired, suggesting that individuals homozygous for H141Y may be predisposed to disease.
authors: Division of Chemistry, Graduate School of Engineering Science, Osaka University, Osaka, Japan.
authors: Jung In
authors: JI
authors: Kim
authors: Division of Chemistry, Graduate School of Engineering Science, Osaka University, Osaka, Japan.
authors: Kosuke
authors: K
authors: Tohashi
authors: Division of Chemistry, Graduate School of Engineering Science, Osaka University, Osaka, Japan.
authors: Shigenori
authors: S
authors: Iwai
authors: Division of Chemistry, Graduate School of Engineering Science, Osaka University, Osaka, Japan.
authors: Isao
authors: I
authors: Kuraoka
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D055162:Biocatalysis; D006720:Homozygote; D006801:Humans; D007288:Inosine / Q000378:metabolism*; D009154:Mutation; D012260:Ribonucleases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D007288:Inosine; D012260:Ribonucleases
keywords: RNA editing; endonuclease V; inosine