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Literature summary 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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.143 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 ?
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 ?
3.2.1.143 poly(ADP-ribosyl)ated-Hrp38 + H2O Drosophila melanogaster
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 ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.143 Drosophila melanogaster
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-
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.143 eye
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 Drosophila melanogaster
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.143 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 ?
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 ?
3.2.1.143 additional information the enzyme cannot hydrolyze the bond between terminal ADP-ribose and glutamate residues of automodifed PARP1 Drosophila melanogaster ?
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 ?
3.2.1.143 poly(ADP-ribosyl)ated-Hrp38 + H2O
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 Drosophila melanogaster ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.143 PARG
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 Drosophila melanogaster

General Information

EC Number General Information Comment Organism
3.2.1.143 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
3.2.1.143 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