| Chapter title |
Quantitative Determination of MAR Hydrolase Residue Specificity In Vitro by Tandem Mass Spectrometry
|
|---|---|
| Chapter number | 19 |
| Book title |
ADP-ribosylation and NAD+ Utilizing Enzymes
|
| Published in |
Methods in molecular biology, August 2018
|
| DOI | 10.1007/978-1-4939-8588-3_19 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-8587-6, 978-1-4939-8588-3
|
| Authors |
Robert Lyle McPherson, Shao-En Ong, Anthony K. L. Leung, McPherson, Robert Lyle, Ong, Shao-En, Leung, Anthony K. L. |
| Abstract |
ADP-ribosylation is a posttranslational modification that involves the conjugation of monomers and polymers of the small molecule ADP-ribose onto amino acid side chains. A family of ADP-ribosyltransferases catalyzes the transfer of the ADP-ribose moiety of nicotinamide adenine dinucleotide (NAD+) onto a variety of amino acid side chains including aspartate, glutamate, lysine, arginine, cysteine, and serine. The monomeric form of the modification mono(ADP-ribosyl)ation (MARylation) is reversed by a number of enzymes including a family of MacroD-type macrodomain-containing mono(ADP-ribose) (MAR) hydrolases. Though it has been inferred from various chemical tests that these enzymes have specificity for MARylated aspartate and glutamate residues in vitro, the amino acid and site specificity of different family members are often not unambiguously defined. Here we describe a mass spectrometry-based assay to determine the site specificity of MAR hydrolases in vitro. |
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