EC Number |
General Information |
Reference |
---|
3.2.1.143 | evolution |
canonical poly(ADP-ribose) glycohydrolase is a highly conserved protein found in organisms ranging from protozoa to humans, phylogenetic analysis. The full-length enzyme from Tetrahymena thermophila is highly similar to the minimal catalytic region of thhe human enzyme, but it lacks the obvious RS/MTS motif |
732568 |
3.2.1.143 | evolution |
conservation of key residues involved in the catalytic process |
732734 |
3.2.1.143 | evolution |
conservation of overall fold amongst mammalian enzyme glycohydrolase domains, additional flexible regions in the catalytic site, overview |
732714 |
3.2.1.143 | evolution |
full-length ARH3 (ARH3FL) adopts a compact all-alpha-helical fold with a central deep ADPR-binding cleft, a signature of the ARH3 superfamily |
754165 |
3.2.1.143 | evolution |
function and domain architecture of human ADP-ribosylation removing enzymes, overview. The key poly(ADP-ribose) (PAR) processing enzyme, PARG, emerged only recently |
754710 |
3.2.1.143 | malfunction |
a deficiency in PARG glycohydrolase activity prolongs DNA damage foci, containing PAR, and similarly delays DNA repair, causing hypersensitivity to DNA damaging agents and selective killing of repair-deficient tumors such as BRCA mutated breast cancers-deficient cancer cells in a manner similar to PARP inhibition |
754122 |
3.2.1.143 | malfunction |
benzo(a)pyrene induces the cell cycle in enzyme-suppressed shPARG cells, phenotype, overview |
731761 |
3.2.1.143 | malfunction |
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses |
-, 754824 |
3.2.1.143 | malfunction |
enzyme deficiency leads to cell death whilst enzyme depletion causes sensitisation to certain DNA damaging agents |
732714 |
3.2.1.143 | malfunction |
genetic disruption of the enzyme leads to increased level of cell death by accumulation of poly(ADP-ribose) |
731453 |