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 followingthe 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).

Snapshots of the reaction mechanism of matrix metalloproteinases / I. Bertini; V. Calderone; M. Fragai; C. Luchinat; M. Maletta; K. J. Yeo. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 45:(2006), pp. 7952-7955. [10.1002/anie.200603100]

Snapshots of the reaction mechanism of matrix metalloproteinases

BERTINI, IVANO;CALDERONE, VITO;FRAGAI, MARCO;LUCHINAT, CLAUDIO;MALETTA, MASSIMILIANO;YEO, KWON JOO
2006

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 followingthe 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).
2006
45
7952
7955
I. Bertini; V. Calderone; M. Fragai; C. Luchinat; M. Maletta; K. J. Yeo
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/354220
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