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Wiley, Angewandte Chemie International Edition, 47(45), p. 7952-7955, 2006

DOI: 10.1002/anie.200603100

Wiley, Angewandte Chemie, 47(118), p. 8120-8123, 2006

DOI: 10.1002/ange.200603100

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Snapshots of the Reaction Mechanism of Matrix Metalloproteinases

This paper is available in a repository.
This paper is available in a repository.

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Abstract

(Figure Presented) 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).