The assimilation of amino acids by bacteria. 24. Inhibitors of incorporation of glycine in disrupted staphylococcal cells

Abstract

The incorporation of glycine by disrupted staphylococcal cells, incubated with a source of energy and (C14-giycine only, is inhibited by 8-hydroxyquinoline (oxine) but not by ethylenediaminetetraacetic acid. The maximal inhibitory concentration of oxine is 10-5[image], higher concentrations being less inhibitory. This concentration abolishes the stimulation of incorporation produced by the addition of nucleic acid to the nucleic acid-depleted preparation. Oxine is not inhibitory in media from which heavy metals have been removed. Benzimidazole is a weak inhibitor whose activity is markedly increased by substitution with CH3- or Cl- in positions 4, 5 and 6. The inhibitory activity of 5,6-dimethylbenzimidazole is increased by substitution with an allyl group in position 1, but similar substitution with [beta]-D-ribofurnanosyl, [beta]-D-glucopyranosyl or 2,3-dihydroxypropyl groups abolishes inhibitory activity. 6-Amino-4-hydroxybenzimidazole and 6-amino-4-hydroxybenzimidazole and 6-amino-4-hydroxybenzotriazole stimulate the incorporation of glycine and antagonize the inhibition by 5,6-dimethylbenzimidazole, l-allyl-5,6-dimethylbenzimidazole and oxine. Analogs of 4,5-diamino-l,2-dimethylbenzene are inhibitors of the incorporation of glycine. The most potent inhibitor found is 1,2-dichloro-5-nitro-4-(p-nitrobenzenesulfonamido) benzene. Chlortetra-cycline, oxytetracycline, penicillin, ethidum bromide, pentamidine and acriflavin inhibit the incorporation of glycine; streptomycin, suramin and isoaniazid are among inactive substances tested.