Development of a clickable activity-based protein profiling (ABPP) probe for agmatine deiminases. Issue 9 (1st May 2015)

• Record Type: Journal Article
• Authors: Marchenko, Mikhail; Thomson, Andrew; Ellis, Terri N.; Knuckley, Bryan; Causey, Corey P.
• Is Part Of: Bioorganic & medicinal chemistry. Volume 23:Issue 9(2015)
• Page Start: 2159
• Page End: 2167
• Publication Date: 2015-05-01
• Subjects: Agmatine deiminase -- Agmatine catabolism -- Activity-based protein profiling -- ABPP probe; Bioorganic chemistry -- Periodicals; Pharmaceutical chemistry -- Periodicals; Biochemistry -- Periodicals; Chemistry, Clinical -- Periodicals; Chemistry, Organic -- Periodicals; Chimie bio-organique -- Périodiques; Chimie pharmaceutique -- Périodiques; 615.19
• DOI: 10.1016/j.bmc.2015.03.013
• Languages: English
• ISSNs: 0968-0896

Abstract

Graphical abstract: Abstract: Agmatine deiminases (AgDs) catalyze the hydrolytic conversion of agmatine (decarboxylated arginine) to N -carbamoylputrescine with concomitant release of ammonia. These enzymes, which are encoded by some pathogenic bacterial species, confer a competitive survival advantage by virtue of energy production and acid tolerance through agmatine catabolism. Herein we report the development of a clickable activity-based protein profiling (ABPP) probe that targets the AgD encoded by Streptococcus mutans with high selectivity and sensitivity.