Modulation of lysyl oxidase activity toward peptidyl lysine by vicinal dicarboxylic amino acid residues. Implications for collagen cross-linking.

@article{Nagan1994ModulationOL,
  title={Modulation of lysyl oxidase activity toward peptidyl lysine by vicinal dicarboxylic amino acid residues. Implications for collagen cross-linking.},
  author={Narasimhan Nagan and Herbert M. Kagan},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 35},
  pages={22366-71}
}
The substrate specificity of lysyl oxidase has been explored with synthetic oligopeptides. kcat/Km increased with increasing peptide length in Ac-(Gly)n-Lys-(Gly)n-CONH2 (n = 1-5). Using 11-mers as the standard peptide length, Glu immediately N-terminal to Lys increased kcat/Km 8.8-fold over that for the -Lys-Glu- sequence and 4.9-fold over the glutamate-free control. Kinetic constants were significantly less perturbed when Glu was 2 or more residues distant from Lys. Replacement of Glu in -Glu… CONTINUE READING

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