The peptidoglycans of Moraxella glucidolytica and Moraxella lwoffi grown on aliphatic hydrocarbons were isolated. They contained muramic acid, glucosamine, alanine, D-glutamic acid and mesodiaminoimelic acid in a molar ratio of about 0.5:0.5:1.6:1.0:1.0 (M. glucidolytica) and 0.8:0.7:1.3:1.0:1.0 (M. lwoffi). The peptidoglycans were lysozyme-resistant. However, when treated with formanide, they could be partially degraded by lysozyme. The fragments were purified and their structure determined. In both strains, the peptide subunits consisted mainly of tripeptides (L-Ala-D-Glu-meso-DAP) and tetrapeptides (L-Ala-D-glu-meso-DAP-D-Ala), most of them being directly cross-linked. It is concluded that in both strains the primary structures of the peptidoglycans are closely related.