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Literature summary extracted from

  • Drown, B.S.; Shirai, T.; Rack, J.G.M.; Ahel, I.; Hergenrother, P.J.
    Monitoring poly(ADP-ribosyl)glycohydrolase activity with a continuous fluorescent substrate (2018), Cell Chem. Biol., 25, 1562-1570 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.2.19 in complex with product ADP-ribose. The interactions of the adenosine and proximal ribose occur primarily through quasidomain D due to a relative movement of the adenosine moiety by 8.4 A and a rotation of about 105°. Comparison with ADP-ribose glycohydrolase ARH3 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.2.19 additional information The activity is abolished upon mutation of even a single Mg2+ coordinating residue Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.19 ADP-ribose
-
 Homo sapiens
3.2.2.19 CaCl2
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.2.19 Mg2+ required. The presence of both Mg2+ ions is required for the correct positioning of the distal ribose. The activity is abolished upon mutation of even a single Mg2+ coordinating residue Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.19 Homo sapiens P54922
-
-

Synonyms

EC Number Synonyms Comment Organism
3.2.2.19 ADPRH
-
 Homo sapiens
3.2.2.19 ARH1
-
 Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.2.2.19 0.164
-
 pH 7.4, temperature not specified in the publication Homo sapiens CaCl2
3.2.2.19 0.228
-
 pH 7.4, temperature not specified in the publication Homo sapiens ADP-ribose