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Research was conducted to examine the in vitro synthesis of peptidoglycan precursors modified with N-acetylputrescine by cyanophora paradoxa cyanelle envelope membranes. Experiments were performed with (1,4-(super 14)C)putrescine as a substrate for the modification reaction. Results demonstrate that the lipid-linked steps of peptidoglycan biosynthesis as well as the putrescinylation and acelation transpiring at the stage of lippid I and/or lipid II were catalyzed by cyanelle envelope membrane preparations.

The modification of D-glutamic acid residues in cyanelle peptidoglycan with N-acetylputrescine (NAP) was detected in Cyanophora paradoxa, Glaucocystis nostochinearum and Cyanoptyche gloeocystis. NAP mediates protein diffusion in glaucocystophyte algae and Cyanophora paradoxa by reducing the polarity of cyanelle peptidoglycan. Furthermore, Glausocystis nostochinearum exhibited a similar muropeptide pattern compared to Cyanophora paradoxa.

The Cyanophora paradoxa cyanell peptidoglycan has a moderately complex primary structure. Muropeptide separation revealed the presence of four distinct muropeptide monomers. Aside from these, 8 dimers, 11 trimers and six tetramers were also detected and subjected to characterization studies. Average glycan chain length was estimated at 50.8 plus-minus 2.6t disaccharide units.