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Literature summary extracted from

  • Barkauskaite, E.; Jankevicius, G.; Ahel, I.
    Structures and mechanisms of enzymes employed in the synthesis and degradation of PARP-dependent protein ADP-ribosylation (2015), Mol. Cell, 58, 935-946 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.143 poly(ADP-ribose) + H2O Homo sapiens
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Organism

EC Number Organism UniProt Comment Textmining
3.2.1.143 Homo sapiens Q86W56
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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 structure of poly(ADP-ribose) glycohydrolase (PARG) in complex with the poly(ADP-ribose) (PAR) substrate reveals that PARG-PAR contacts are provided almost exclusively by the macrodomain. The accessory domain (which is part of the PARG catalytic region) has only limited interaction with PAR, but it structurally supports the PARG catalytic loop and may have an important role in regulation of PARG catalytic activity. The PARG-PAR structure also reveals that PARGs preferably bind PAR at the chain termini and primarily act as exo-glycohydrolases (whereby PARG sequentially degrades terminal ADP-ribose units). While binding along the PAR chain and endo-glycohydrolytic cleavage of PAR is structurally possible, it appears to be less efficient. Due to active site constraints and the conformation of bound PAR, canonical PARGs are unlikely to efficiently bind the aforementioned putative PAR branch sites Homo sapiens ?
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3.2.1.143 poly(ADP-ribose) + H2O
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 Homo sapiens ?
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3.2.1.143 poly(ADP-ribose) + H2O PAR Homo sapiens ?
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Subunits

EC Number Subunits Comment Organism
3.2.1.143 More human as well as other vertebrate PARGs are composed of three domains: two of these domains, namely macrodomain and the PARG accessory domain, make up the minimal PARG catalytic region, while the third domain, which shows significantly less sequence conservation, is the putative PARG regulatory region. The latter regulatory domain is absent in PARGs of the majority of eukaryotes, and it is not important for PAR hydrolysis in vitro Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.2.1.143 PAR glycohydrolase
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 Homo sapiens
3.2.1.143 PARG
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 Homo sapiens

General Information

EC Number General Information Comment Organism
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 Homo sapiens
3.2.1.143 metabolism PARP-dependent ADP-ribosylation cycle involving enzyme PARG Homo sapiens
3.2.1.143 physiological function the poly(ADP-ribose) glycohydrolase (PARG) endo-glycohydrolase activity may become significant in vivo at high PAR/PARG ratios (for example, in the case of an extreme cellular insult), thus releasing free PAR fragments to mediate apoptotic signaling Homo sapiens