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. 1974 Sep;119(3):805–810. doi: 10.1128/jb.119.3.805-810.1974

Initiation of Spore Germination in Bacillus subtilis: Relationship to Inhibition of l-Alanine Metabolism

Chandan Prasad a,1
PMCID: PMC245684  PMID: 4212093

Abstract

The inhibitory effects of anthranilic acid esters (methyl anthranilate and N-methyl anthranilate) on the l-alanine-induced initiation of spore germination was examined in Bacillus subtilis 168. Methyl anthranilate irreversibly inhibited alanine initiation by a competitive mechanism. In its presence, the inhibition could be reversed only by the combined addition of d-glucose, d-fructose, and K+. Both l-alanine dehydrogenase and l-glutamate-pyruvate transaminase, enzymes which catalyze the first reaction in l-alanine metabolism, were competitively inhibited by methyl anthranilate. The Ki values for germination initiation (0.053 mM) and of l-glutamate-pyruvate transaminase (0.068 mM) were similar, whereas that for l-alanine dehydrogenase (0.4 mM) was six to seven times higher. Since a mutant lacking l-alanine dehydrogenase activity germinated normally in l-alanine alone, it is speculated that the major pathway of l-alanine metabolism during initiation may be via transmination reaction.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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