Development of a clickable activity-based protein profiling (ABPP) probe for agmatine deiminases

Authors

Mikhail Marchenko, University of North Florida
Andrew Thomson, University of North Florida
Terri N. Ellis, University of North FloridaFollow
Bryan Knuckley, University of North FloridaFollow
Corey P. Causey, University of North FloridaFollow

Document Type

Article

Publication Date

5-1-2015

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.

Publication Title

Bioorganic and Medicinal Chemistry

Volume

23

Issue

9

First Page

2159

Last Page

2167

Digital Object Identifier (DOI)

10.1016/j.bmc.2015.03.013

PubMed ID

25819331

ISSN

09680896

E-ISSN

14643391

Citation Information

Marchenko, Thomson, A., Ellis, T. N., Knuckley, B., & Causey, C. P. (2015). Development of a clickable activity-based protein profiling (ABPP) probe for agmatine deiminases. Bioorganic & Medicinal Chemistry, 23(9), 2159–2167. https://doi.org/10.1016/j.bmc.2015.03.013