Site-specific cleavage--a model system for the identification of lipid-modified glutamate residues in proteins.

Numerous proteins are modified post-translationally after their biosynthesis at the ribosomes of the cell. One such modification, only poorly characterized to date, is the formation of lipid esters of glutamate side chains in the skin proteins of land-living mammals; here a subset of very long chain fatty acids, ceramides and/or glucosylceramides, are bound through their omega-hydroxy groups to structural proteins of the so-called "cornified envelope" in the outermost layer of the skin, the stratum corneum. We report an approach for the identification of proteins containing ester-modified glutamic acid residues and the determination of their positions within the peptide sequence, designed for mass spectrometric investigation of human skin proteins.