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Literature summary 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

Crystallization (Commentary)

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

Protein Variants

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.143 ADP-HPD
-
Homo sapiens

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
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.143 Homo sapiens Q86W56
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.143 2'-O-(ADP-ribosyl)-adenosine 5'-phosphate + H2O
-
Homo sapiens ?
-
?
3.2.1.143 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
-
?
3.2.1.143 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 ?
-
?
3.2.1.143 poly(ADP-ribose) + H2O
-
Homo sapiens ?
-
?
3.2.1.143 propargyl ADP-ribose dimer + H2O
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Homo sapiens propargyl ADP-ribose + ADP-ribose
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.143 PARG
-
Homo sapiens

General Information

EC Number General Information Comment Organism
3.2.1.143 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