Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases.

By A. Anders, S. Gilbert, W. Garten, R. Postina, F. Fahrenholz. 2001

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A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “The pro-protein convertase then adds Zn2+ coordination to the metalloprotease domain so that ADAM can be catalytically activated and perform its physiological function and sheddase activity [28].”
The ADAM metalloproteinases (2008, background): “…the Cys-switch mechanism involved in maintaining latency (Gonzales et al., 2004), and indeed it has been suggested that the main functions of the pro-domain are to act as a chaperone and to protect the enzymes from degradation in the secretory system (Anders et al., 2001; Milla et al., 2006).”
Strategies to improve plasma half life time of peptide and protein drugs (2006, background): “81 endopeptidase of broad specificity Membrane (kidney) (Anders et al., 2001) 3.”