Snapshots of the Reaction Mechanism of Matrix Metalloproteinases

Abstract

The series of events that occur in the catalytic cycle of matrix metalloproteinases were modeled on the basis of X-ray crystal structures of the active, uninhibited enzymes and of the same enzymes following the hydrolysis of a peptide substrate. After the peptide bond has been broken, both peptide fragments remain bound to the protein initially (see structure of the active-site cavity of the enzyme MMP-12 immediately after substrate hydrolysis). Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2006/z603100_s.html or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.