title: Synthesis and evaluation of 2-ethynyl-adenosine-5'-triphosphate as a chemical reporter for protein AMPylation.
abstract: Protein AMPylation is a posttranslational modification (PTM) defined as the transfer of an adenosine monophosphate (AMP) from adenosine triphosphate (ATP) to a hydroxyl side-chain of a protein substrate. One recently reported AMPylator enzyme, Vibrio outer protein S (VopS), plays a role in pathogenesis by AMPylation of Rho GTPases, which disrupts crucial signaling pathways, leading to eventual cell death. Given the resurgent interest in this modification, there is a critical need for chemical tools that better facilitate the study of AMPylation and the enzymes responsible for this modification. Herein we report the synthesis of 2-ethynyl-adenosine-5'-triphosphate () and its utilization as a non-radioactive chemical reporter for protein AMPylation.
authors.affiliation: Department of Chemistry, University of North Florida, 1 UNF Drive, Jacksonville, FL 32224, USA. corey.causey@unf.edu.
authors.forename: Christa
authors.initials: C
authors.lastname: Creech
authors.forename: Mukul
authors.initials: M
authors.lastname: Kanaujia
authors.forename: Corey P
authors.initials: CP
authors.lastname: Causey
mesh_terms: D000249:Adenosine Monophosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000138:chemical synthesis* / Q000737:chemistry*; D001710:Biotin / Q000737:chemistry / Q000378:metabolism; D060326:Chemistry Techniques, Synthetic; D015195:Drug Design; D005456:Fluorescent Dyes / Q000138:chemical synthesis* / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D020764:cdc42 GTP-Binding Protein / Q000737:chemistry / Q000378:metabolism
chemical_list: C000607230:2-ethynyl-adenosine-5'-triphosphate; D005456:Fluorescent Dyes; D000249:Adenosine Monophosphate; D001710:Biotin; D000255:Adenosine Triphosphate; D020764:cdc42 GTP-Binding Protein