Modulation of lysyl oxidase-like 2 enzymatic activity by an allosteric antibody inhibitor.

@article{Rodriguez2010ModulationOL,
  title={Modulation of lysyl oxidase-like 2 enzymatic activity by an allosteric antibody inhibitor.},
  author={Hector M. Rodriguez and Maria Vaysberg and Amanda J Mikels and Scott A McCauley and Arleene C. Velayo and Carlos Garc{\'i}a and Victoria Smith},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 27},
  pages={20964-74}
}
In this report, we assessed the steady-state enzymatic activity of lysyl oxidase-like 2 (LOXL2) against the substrates 1,5-diaminopentane (DAP), spermine, and fibrillar type I collagen. We find that both DAP and spermine are capable of activating LOXL2 to the same extent and have similar Michaelis constants (K(m) approximately 1 mm) and catalytic rates (k(cat) approximately 0.02 s(-1)). We also show that LOXL2 is capable of being inhibited by a known suicide inhibitor of lysyl oxidase (LOX… CONTINUE READING

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