CBA-4 is an L,D-transpeptidase inhibitor. CBA-4 covalently acylates the active site of L,D-transpeptidase to form a stable acylenzyme adduct. CBA-4 can be used for research on bacterial resistance [1].
In Vitro, CBA-4 (39 μM; 15 min) fully acylates purified Ldtfm and forms a stable acyl-enzyme adduct that shows no detectable hydrolysis after 3 h of incubation[1]. CBA-4 (30 min) undergoes copper-catalyzed azide–alkyne cycloaddition (CuAAC) with 3-azido-7-hydroxycoumarin at an initial rate of 0.56 μM min−1, reaching 21% conversion after 30 min of incubation at room temperature[1].
References:
[1]. Saidjalolov S, et al. Click and Release Chemistry for Activity-Based Purification of β-Lactam Targets. Chemistry. 2021 May 17;27(28):7687-7695.
In Vitro, CBA-4 (39 μM; 15 min) fully acylates purified Ldtfm and forms a stable acyl-enzyme adduct that shows no detectable hydrolysis after 3 h of incubation[1]. CBA-4 (30 min) undergoes copper-catalyzed azide–alkyne cycloaddition (CuAAC) with 3-azido-7-hydroxycoumarin at an initial rate of 0.56 μM min−1, reaching 21% conversion after 30 min of incubation at room temperature[1].
References:
[1]. Saidjalolov S, et al. Click and Release Chemistry for Activity-Based Purification of β-Lactam Targets. Chemistry. 2021 May 17;27(28):7687-7695.