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Properties and function of lysyl oxidase.

H M Kagan1, P C Trackman

  • 1Department of Biochemistry, Boston University School of Medicine, Massachusetts.

American Journal of Respiratory Cell and Molecular Biology
|September 1, 1991
PubMed
Summary

Lysyl oxidase is crucial for stabilizing collagen and elastin fibers by crosslinking. Its mechanism involves copper and a quinone cofactor, and it can be inhibited by certain amines.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Connective Tissue Biology

Background:

  • Lysyl oxidase (LOX) is essential for the structural integrity of connective tissues.
  • LOX facilitates the formation of covalent crosslinks in collagen and elastin fibers.
  • LOX activity is implicated in fibrotic and malignant diseases.

Purpose of the Study:

  • To elucidate the catalytic mechanism of lysyl oxidase.
  • To investigate the role of copper and o-quinone cofactors in LOX activity.
  • To discuss LOX regulation in disease contexts.

Main Methods:

  • Analysis of kinetic and chemical data.
  • Evaluation of mechanism-based inhibition by monoamines and diamines.
  • Review of recent evidence on LOX biosynthesis and regulation.

Main Results:

  • Proposed a mechanism of action for lysyl oxidase based on available data.
  • Identified copper and an o-quinone cofactor.
  • Demonstrated that specific amines can inhibit the enzyme.
  • Highlighted recent findings on LOX precursors and disease-related regulation.

Conclusions:

  • The proposed mechanism explains LOX function and inhibition.
  • LOX plays a significant role in tissue structure and disease pathology.
  • Further research into LOX regulation is critical for therapeutic strategies.

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