Hydrolysis of O-Acetyl-ADP-ribose Isomers by ADP-ribosylhydrolase 3
نویسندگان
چکیده
منابع مشابه
Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3.
O-acetyl-ADP-ribose (OAADPr), produced by the Sir2-catalyzed NAD(+)-dependent histone/protein deacetylase reaction, regulates diverse biological processes. Interconversion between two OAADPr isomers with acetyl attached to the C-2″ and C-3″ hydroxyl of ADP-ribose (ADPr) is rapid. We reported earlier that ADP-ribosylhydrolase 3 (ARH3), one of three ARH proteins sharing structural similarities, h...
متن کاملHydrolysis of O-Acetyl-ADP-ribose Isomers
O-Acetyl-ADP-ribose (OAADPr), produced by the Sir2-catalyzed NAD -dependent histone/protein deacetylase reaction, regulates diverse biological processes. Interconversion between two OAADPr isomers with acetyl attached to the C-2 and C-3 hydroxyl of ADP-ribose (ADPr) is rapid. We reported earlier that ADP-ribosylhydrolase 3 (ARH3), one of three ARH proteins sharing structural similarities, hydro...
متن کاملTransition-State Analysis of 2-O-Acetyl-ADP-Ribose Hydrolysis by Human Macrodomain 1
Macrodomains, including the human macrodomain 1 (MacroD1), are erasers of the post-translational modification of monoadenosinediphospho-ribosylation and hydrolytically deacetylate the sirtuin product O-acetyl-ADP-ribose (OAADPr). OAADPr has been reported to play a role in cell signaling based on oocyte microinjection studies, and macrodomains affect an array of cell processes including transcri...
متن کاملStructure of mouse ADP-ribosylhydrolase 3 (mARH3)
ADP-ribosylation is a reversible and covalent post-translational modification in which the attachment of ADP-ribose is catalyzed by ADP-ribosyltransferases and the removal of ADP-ribose is catalyzed by ADP-ribosylhydrolases. ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. The three-dimensional structure has been resolved at a...
متن کاملSynthesis and biochemical evaluation of O-acetyl-ADP-ribose and N-acetyl analogs.
Synthetic routes for the preparation of O-acetyl-ADP-ribose and two novel non-hydrolyzable analogs containing an N-acetyl are described and shown to interact with the macro domain of histone protein H2A1.1.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m111.237636