The Structural Basis for the Elastolytic Activity of the 92-kDa and 72-kDa Gelatinases ROLE OF THE FIBRONECTIN TYPE II-LIKE REPEATS

摘要: Several matrix metalloproteinases, including the 92-kDa and 72-kDa gelatinases, macrophage metalloelastase (MME), matrilysin degrade insoluble elastin. Because elastolytically active MME consist only of a catalytic domain (CD), we speculated that homologous CDs gelatinases would confer their elastolytic activities. In contrast to CD, 92 72 expressed in Escherichia coli (lacking internal fibronectin type II-like repeats) had no elastase activity, although both were gelatinolytic cleaved thiopeptolide substrate at rates comparable full-length gelatinases. To test role repeats gelatinase CD with its (92 CD/FN) yeast. CD/FN degraded elastin activity gelatinase. lacking did not bind elastin, whereas parent enzymes Furthermore, recombinant inhibited binding We conclude 92- require for activity.