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Literature summary for 3.1.21.7 extracted from

  • Kim, J.; Tohashi, K.; Iwai, S.; Kuraoka, I.
    Inosine-specific ribonuclease activity of natural variants of human endonuclease V (2016), FEBS Lett., 590, 4354-4360 .
No PubMed abstract available
Search for more literature for 3.1.21.7

Protein Variants

Protein Variants Comment Organism
D201N the mutant enzyme has comparable RNase activity as wild-type enzyme Homo sapiens
H141Y the mutant enzyme is catalytically impaired, it generates less than one-third of the cleavage product produced by wild-type, suggesting that individuals homozygous for H141Y may be predisposed to disease Homo sapiens
K114R the mutant enzyme has comparable RNase activity as wild-type enzyme Homo sapiens
R112Q the mutant enzyme has comparable RNase activity as wild-type enzyme Homo sapiens
V29I the mutant enzyme has comparable RNase activity as wild-type enzyme Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8N8Q3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxyinosine-containing RNA + H2O (32)P-labeled 21-mer RNA substrate with inosine (5'-CUGUAUGAUGIAGAUGCUGAC-3'). EndoV is a deoxyinosine 3'-endonuclease that recognizes DNA containing deoxyinosine, and cleaves the second and third phosphodiester bonds 3' to the damaged base, leaving a nick with 3' hydroxyl and 5' phosphate groups. Human endonuclease V prefers RNA substrates with inosine over DNA substrates with deoxyinosine Homo sapiens ?
-
 ?

General Information

General Information Comment Organism
physiological function 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 Homo sapiens