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

被引:4
作者
Marchenko, Mikhail [1 ]
Thomson, Andrew [1 ]
Ellis, Terri N. [2 ]
Knuckley, Bryan [1 ]
Causey, Corey P. [1 ]
机构
[1] Univ N Florida, Dept Chem, Jacksonville, FL 32224 USA
[2] Univ N Florida, Dept Biol, Jacksonville, FL 32224 USA
关键词
Agmatine deiminase; Agmatine catabolism; Activity-based protein profiling; ABPP probe; STREPTOCOCCUS-MUTANS UA159; GENE-CLUSTER; NITRIC-OXIDE; IN-VITRO; ARGININE; METABOLISM; ACTIVATION; RECEPTORS; DISCOVERY; DESIGN;
D O I
10.1016/j.bmc.2015.03.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2159 / 2167
页数:9
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