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Literature summary for 3.2.1.143 extracted from

  • Lambrecht, M.J.; Brichacek, M.; Barkauskaite, E.; Ariza, A.; Ahel, I.; Hergenrother, P.J.
    Synthesis of dimeric ADP-ribose and its structure with human poly(ADP-ribose) glycohydrolase (2015), J. Am. Chem. Soc., 137, 3558-3564 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.143

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in complex with ADP-ribose dimer, X-ray diffraction structure determination and analysis at 1.9 A resolution Homo sapiens

Protein Variants

Protein Variants Comment Organism
E755N site-directed mutagenesis, inactive mutant Homo sapiens
E756N site-directed mutagenesis, inactive mutant Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
ADP-HPD
-
 Homo sapiens

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.
2'-O-(ADP-ribosyl)-adenosine 5'-phosphate + H2O
-
 Homo sapiens ?
-
 ?
ADP-ribose dimer + H2O the N-1 adenine group interacts with the amide nitrogen of the conserved Leu752 in human PARG, while the beta-phosphate forms H-bonds with the conserved Ala750, enzyme-substrate binding structure, crystal structure analysis, overview Homo sapiens 2 ADP-ribose
-
 ?
additional information synthesis of derivatives of the ADP-ribose dimer and development of a PAR Binding assay, overview. Propargyl ADP-ribose dimer binds to E756N and E755N mutants of human PARG with KD values of 83 nM and 208 nM, respectively. Fluorescent propargyl ADP-ribose dimer does not bind proteins devoid of PAR binding activity such as bovine serum albumin even at high concentrations of protein. Wild-type PARG is unable to process the truncated substrates 2'-O-alpha-D-ribofuranosyladenosine and 2'-O-(5-O-phosphono-a-D-ribofuranosyl)adenosine 5'-phosphate) Homo sapiens ?
-
 ?
poly(ADP-ribose) + H2O
-
 Homo sapiens ?
-
 ?
propargyl ADP-ribose dimer + H2O
-
 Homo sapiens propargyl ADP-ribose + ADP-ribose
-
 ?

Synonyms

Synonyms Comment Organism
PARG
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function poly(ADP-ribosyl)ation is a common post-translational modification that mediates a wide variety of cellular processes including DNA damage repair, chromatin regulation, transcription, and apoptosis, involving interactions of PAR with poly(ADP-ribose) glycohydrolase (PARG) and other binding proteins Homo sapiens