Catalytic properties and structural components of lysyl oxidase.

Key aspects of the biosynthesis and catalytic specificity of lysyl oxidase (LO) have been explored. Oxidation of peptidyl lysine in synthetic oligopeptides is markedly sensitive to the presence of vicinal dicarboxylic ami/no acid residues. Optimal activity is obtained with the -Glu-Lys- sequence within a polyglycine 11-mer, whereas the -Lys-Glu- sequence is much less efficiently oxidized. The -Asp-Glu-Lys- sequence is a very poor substrate, although this sequence is oxidized in type I collagen fibrils. These results are considered in the light of a model requiring collagen to be assembled as fibrils prior to oxidation by LO. An in vitro system for the expression of catalytically active LO has been devised. Deletion or inclusion of the cDNA coding for the propeptide region in the expressed construct results in apparently identical, catalytically active enzyme products, indicating the lack of essentiality of this region for active enzyme production. These effects are considered with respect to the conservation of the amino acid sequence of LO produced by different species.