Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the N-terminal regulatory fragment can activate in trans the inactive enzyme fragment depleted with this segment. This suggests that, whereas the enzyme activity can be inhibited by disrupting the docking of this segment to its enzyme binding groove (via posttranslational modification or protein-proteins interactions), the enzyme can be reversibly activated once the disruptive factor is removed | Mus musculus |
Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a target for development of specific inhibitors | Mus musculus |
Crystallization (Comment) | Organism |
---|---|
enzyme catalytic domain free or in complexes with ADP-ribose and inhibitor ADP-HPD, as well as four enzyme catalytic residues mutants, X-ray diffraction structure determination and analysis | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
E748N | site-directed mutagenesis, the mutant is inactive, activity is disrupted due to significant conformational changes | Mus musculus |
E748Q | site-directed mutagenesis, the mutant activity is highly reduced compared to the wild-type enzyme | Mus musculus |
E749N | site-directed mutagenesis, the mutant is inactive, activity is disrupted due to significant conformational changes | Mus musculus |
E749Q | site-directed mutagenesis, the mutant activity is highly reduced compared to the wild-type enzyme | Mus musculus |
F868A | site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme | Mus musculus |
G737A/G738A | site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme | Mus musculus |
G866A | site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
adenosine 5'-diphosphate-(hydroxymethyl)-pyrrolidinediol | ADP-HPD, an analogue of ADP-ribose | Mus musculus | |
additional information | the N-terminal regulatory fragment can activate in trans the inactive enzyme fragment depleted with this segment. This suggests that, whereas the enzyme activity can be inhibited by disrupting the docking of this segment to its enzyme binding groove (via posttranslational modification or protein-proteins interactions), the enzyme can be reversibly activated once the disruptive factor is removed | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
poly(ADP-D-ribose)n + H2O | Mus musculus | - |
poly(ADP-D-ribose)n-1 + ADP-ribose | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | O88622 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose | catalytic mechanism, structure-function analysis, overview | Mus musculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
poly(ADP-D-ribose)n + H2O | - |
Mus musculus | poly(ADP-D-ribose)n-1 + ADP-ribose | - |
? | |
poly(ADP-D-ribose)n + H2O | binding structure of ADP-ribose to wild-type and mutant enzymes, overview | Mus musculus | poly(ADP-D-ribose)n-1 + ADP-ribose | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PARG | - |
Mus musculus |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.00012 | - |
pH and temperature not specified in the publication | Mus musculus | adenosine 5'-diphosphate-(hydroxymethyl)-pyrrolidinediol |
General Information | Comment | Organism |
---|---|---|
additional information | E748 and E749 are the key catalytic residues in the signature loop, N733 directly recognizes the 3'-OH on the proximal ribose, catalytic domain structure in apo- and liganded-states, overview. The N-terminal flexible peptide preceding the enzyme's catalytic domain may regulate the enzymatic activity, catalytic and regulatory mechanisms, overview. A binding site outside of the catalytic cleft for iso-ADP-ribose, which is probably the smallest enzyme subtrate containing the alpha(1->2) ribose-ribose glycosidic bond, may explain the processivity of the enzyme activity | Mus musculus |
physiological function | protein poly(ADP-ribosyl)ation regulates a number of important cellular processes. Poly(ADP-ribose) glycohydrolase is the primary enzyme responsible for hydrolyzing the poly(ADP-ribose) polymer in vivo | Mus musculus |