Design, synthesis, and in vitro evaluation of an activity-based protein profiling (ABPP) probe targeting agmatine deiminases
Document Type
Article
Publication Date
9-1-2014
Abstract
Agmatine deiminases (AgDs) belong to a family of enzymes known as guanidinium group modifying enzymes (GMEs). Many pathogenic bacteria encode an AgD that participates in the catabolism of agmatine (decarboxylated arginine). This catabolism may confer a competitive survival advantage, by virtue of energy production and increased acid tolerance, making this sub-family of enzymes a potential therapeutic target that warrants further study. Herein we report the development of an activity-based protein profiling (ABPP) probe that selectively targets the AgD from Streptococcus mutans. Due to the selectivity and covalent nature of the modification, this probe could prove to be a valuable tool for the study of other AgD family members. © 2014 Elsevier Ltd. All rights reserved.
Publication Title
Bioorganic and Medicinal Chemistry
Volume
22
Issue
17
First Page
4602
Last Page
4608
Digital Object Identifier (DOI)
10.1016/j.bmc.2014.07.028
PubMed ID
25127464
ISSN
09680896
E-ISSN
14643391
Citation Information
Thomson, O’Connor, S., Knuckley, B., & Causey, C. P. (2014). Design, synthesis, and in vitro evaluation of an activity-based protein profiling (ABPP) probe targeting agmatine deiminases. Bioorganic & Medicinal Chemistry, 22(17), 4602–4608. https://doi.org/10.1016/j.bmc.2014.07.028