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ADPRHL2  -  ADP-ribosylhydrolase like 2

Homo sapiens

Synonyms: ADP-ribosylhydrolase 3, ARH3, FLJ20446, Poly(ADP-ribose) glycohydrolase ARH3
 
 
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High impact information on ADPRHL2

  • Recombinant hARH3 binds free ADP-ribose with micromolar affinity and efficiently de-ADP-ribosylates poly- but not monoADP-ribosylated proteins [1].
  • The rate of O-acetyl-ADP-ribose hydrolysis by recombinant ARH3 was 250-fold that observed with ARH1; ARH2 and poly(ADP-ribose) glycohydrolase were inactive [2].
  • ARH1 was reported to hydrolyze ADP-ribosylarginine, whereas ARH3 degraded poly(ADP-ribose) [2].
  • Like the degradation of poly(ADP-ribose) by ARH3, hydrolysis of O-acetyl-ADP-ribose was abolished by replacement of the vicinal aspartates at positions 77 and 78 of ARH3 with asparagine [2].
  • All findings are consistent with the conclusion that ARH3 has PARG activity but is structurally unrelated to PARG [3].
 

Biological context of ADPRHL2

 

Associations of ADPRHL2 with chemical compounds

  • We report here the identification of an ARH1-like protein, termed poly(ADP-ribose) hydrolase or ARH3, which exhibited PARG activity, generating ADP-ribose from poly-(ADP-ribose), but did not hydrolyze ADP-ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds [3].
  • ARH3 activity, like that of ARH1, was enhanced by Mg(2+) [3].
 

Analytical, diagnostic and therapeutic context of ADPRHL2

  • Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase [4].

References

  1. The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation. Mueller-Dieckmann, C., Kernstock, S., Lisurek, M., von Kries, J.P., Haag, F., Weiss, M.S., Koch-Nolte, F. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases. Ono, T., Kasamatsu, A., Oka, S., Moss, J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. Oka, S., Kato, J., Moss, J. J. Biol. Chem. (2006) [Pubmed]
  4. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase. Kernstock, S., Koch-Nolte, F., Mueller-Dieckmann, J., Weiss, M.S., Mueller-Dieckmann, C. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
 
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