reviewJournal of Cellular BiochemistryNov 27, 2002Closed access

Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cell

Boston University

PubMed
Indexed incrossrefpubmed

Abstract

Lysyl oxidase (LO) plays a critical role in the formation and repair of the extracellular matrix (ECM) by oxidizing lysine residues in elastin and collagen, thereby initiating the formation of covalent crosslinkages which stabilize these fibrous proteins. Its catalytic activity depends upon both its copper cofactor and a unique carbonyl cofactor and has been shown to extend to a variety of basic globular proteins, including histone H1. Although the three-dimensional structure of LO has yet to be determined, the present treatise offers hypotheses based upon its primary sequence, which may underlie the prominent electrostatic component of its unusual substrate specificity as well as the catalysis-suppressing…

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940
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Authors

2

Topics & keywords

Keywords
  • Lysyl oxidase
  • Elastin
  • Extracellular matrix
  • Lysine
  • Biochemistry
  • Chemistry
  • Cofactor
  • Covalent bond
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