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

BRENDA support

Literature summary for 3.2.1.143 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
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.
poly(ADP-ribose) + H2O Homo sapiens
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q86W56
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
poly(ADP-ribose) + H2O
-
 Homo sapiens ?
-
 ?
poly(ADP-ribose) + H2O PAR Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
PAR glycohydrolase
-
 Homo sapiens
PARG
-
 Homo sapiens

General Information

General Information Comment Organism
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
metabolism PARP-dependent ADP-ribosylation cycle involving enzyme PARG Homo sapiens
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