| Abstract
| - 1-Amino-2-methylenecyclopropane-1-carboxylic acid (2-methylene-ACC) is an irreversible inhibitorfor a bacterial enzyme, 1-aminocyclopropane-1-carboxylate (ACC) deaminase, which catalyzes theconversion of ACC to α-ketobutyrate and ammonia. The inactivation has been proposed to proceedwith the ring scission induced by an addition of an enzyme nucleophile, resulting in the formationof a reactive turnover product that then traps an active-site residue. To gain further insight intothis unique enzymatic reaction, the tritiated 2-methylene-ACC was prepared and incubated withACC deaminase to locate and identify the entrapped amino acid residue. The synthesis of thisradiolabeled compound and the results of its incubation with ACC deaminase are reported in thispaper.
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