The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin

Mol Biol Rep. 2011 Jan;38(1):145-9. doi: 10.1007/s11033-010-0088-0. Epub 2010 Mar 21.


The lysyl oxidase-like 2 (LOXL2) protein is a human paralogue of lysyl oxidase (LOX) that functions as an amine oxidase for formation of lysine-derived cross-links found in collagen and elastin. In addition to the C-terminal domains characteristic to the LOX family members, LOXL2 contains four scavenger receptor cysteine-rich (SRCR) domains in the N-terminus. In order to assess the amine oxidase activity of LOXL2, we expressed a series of recombinant LOXL2 proteins with deletions in the SRCR domains, using an Escherichia coli expression system. All of the purified recombinant LOXL2 proteins, with or without the SRCR domains in the N-terminus, showed significant amine oxidase activity toward several different types of collagen and elastin in in vitro amine oxidase assays, indicating deletion of the SRCR domains does not interfere with amine oxidase activity of LOXL2. Further, amine oxidase activity of LOXL2 was not susceptible to inhibition by β-aminopropionitrile, an irreversible inhibitor of LOX, suggesting a different enzymatic mechanism between these two paralogues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Oxidoreductases / chemistry
  • Amino Acid Oxidoreductases / metabolism*
  • Aminopropionitrile / pharmacology
  • Animals
  • Cattle
  • Collagen / metabolism*
  • Elastin / metabolism*
  • Escherichia coli
  • Humans
  • Oxidoreductases Acting on CH-NH2 Group Donors / chemistry
  • Oxidoreductases Acting on CH-NH2 Group Donors / metabolism*
  • Protein Structure, Tertiary
  • Recombinant Proteins / isolation & purification
  • Substrate Specificity / drug effects


  • Recombinant Proteins
  • Aminopropionitrile
  • Collagen
  • Elastin
  • Amino Acid Oxidoreductases
  • Oxidoreductases Acting on CH-NH2 Group Donors
  • LOXL2 protein, human