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Synthesis and enantioselective mutagenicity of azidoalanine in Salmonella typhimurium

1986; Elsevier BV; Volume: 60; Issue: 2 Linguagem: Inglês

10.1016/0009-2797(86)90026-8

1872-7786

James B. Mangold, James M. LaVelle,

Synthesis and Biological Evaluation

Azide mutagenicity involves the requisite formation of the putative novel aminoacid metabolite, β-azidoalanine. The role of this metabolite, however, is unclear. In order to confirm the identity of this metabolite and provide additional information on possible stereochemical requirements for mutagenicity, authentic racemic and L-azidoalanine were synthesized by an unambiguous route and tested for mutagenicity in Salmonella typhimurium TA100, TA1535, hisG46 and Escherichia coli WP2-. A marked antipodal potency ratio was observed in strains TA100 and TA1535 when racemic and L-azidoalanine were compared. The mutagenic activity resided primarily in the L-isomer. The molar potency of L-azidoalanine in TA100 and TA1535 was nearly identical to that of azide. The lack of mutagenic response for racemic or L-azidoalanine in hisG46 and E. coli WP2- was like that reported for azide and is consistent with similar modes of action for these agents.