(Q24672688)

O-acetyl-ADP-ribose deacetylase activity

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Joel Moss

4

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author name string

Tohru Ono

1

0 references

Atsushi Kasamatsu

2

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Shunya Oka

Proceedings of the National Academy of Sciences of the United States of America

3

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language of work or name

English

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publication date

7 November 2006

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published in

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volume

103

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issue

45

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page(s)

16687-91

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cites work

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The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase

7 April 2017

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SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria

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Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose

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Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity

7 April 2017

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Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase

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Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolases

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Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases

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Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase

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Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product

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Sir2 links chromatin silencing, metabolism, and aging

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Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases

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Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain

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Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes

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Structural identification of 2'- and 3'-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases

30 May 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0607911103

Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0607911103

Glycosylphosphatidylinositol-anchored and secretory isoforms of mono-ADP-ribosyltransferases

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/17075046

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.0607911103

1 reference

ADS bibcode

2006PNAS..10316687O

0 references

1 reference

1 reference

PubMed publication ID

17075046

1 reference