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Summary: A diaminopimelate-requiring mutant of Bacillus megaterium was shown to lack the enzyme N-acetyl-ll-diaminopimelate deacylase. By repeated subculture of this mutant, a second-stage mutant was derived that could grow slowly in minimal defined medium supplemented with dd-diaminopimelate alone. After growth in such medium, the peptidoglycan of the wall still contained mainly meso- and ll-diaminopimelate; radioactivity from dd-diamino-[14C]pimelate entered peptidoglycan (as diamino[14C]pimelate) and protein (as [14C]lysine) to similar extents.

Metabolism of DD-2,6-Diaminopimelic Acid by a Diaminopimelate-requiring Mutant of Bacillus megaterium