Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.143 extracted from

  • Ji, Y.; Jarnik, M.; Tulin, A.V.
    Poly(ADP-ribose) glycohydrolase and poly(ADP-ribose)-interacting protein Hrp38 regulate pattern formation during Drosophila eye development (2013), Gene, 526, 187-194.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.143

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Drosophila melanogaster the enzyme is responsible for the cleavage of poly(ADP-D-ribose) into the single ADP-ribose unit by hydrolyzing the ribose-ribose bonds within the polymer chain ?
-
 ?
poly(ADP-ribosyl)ated-Hrp38 + H2O Drosophila melanogaster
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
eye
-
 Drosophila melanogaster
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is responsible for the cleavage of poly(ADP-D-ribose) into the single ADP-ribose unit by hydrolyzing the ribose-ribose bonds within the polymer chain Drosophila melanogaster ?
-
 ?
additional information the enzyme cannot hydrolyze the bond between terminal ADP-ribose and glutamate residues of automodifed PARP1 Drosophila melanogaster ?
-
 ?
poly(ADP-ribosyl)ated-Hrp38 + H2O
-
 Drosophila melanogaster ?
-
 ?

Synonyms

Synonyms Comment Organism
PARG
-
 Drosophila melanogaster

General Information

General Information Comment Organism
malfunction poly(ADP-ribose) glycohydrolase loss-of-function causes increased Hrp38 poly(ADP-ribosyl)ation and also results in the rough-eye phenotype with disrupted ommatidial lattice and and bristles and reduced number of photoreceptor cells. Hrp38 is essential for fly eye development. Parg mutant eye clones have decreased expression level of DE-cadherin with orientation defects, which is reminiscent of DE-cadherin mutant eye phenotype. The Parg mutant eye accumulates a large amount of poly(ADP-ribose) Drosophila melanogaster
physiological function the enzyme activity regulates cellular poly(ADP-ribose) level. Since the enzyme cannot cleave the terminal ADP-ribose unit at the protein bound to glutamate residues, the residual activities of MacroD2 and TARG1 may contribute to the accumulation of poly(ADP-D-ribose)in the Parg knockout animals Drosophila melanogaster