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Multiple architectures and mechanisms of latency in metallopeptidase zymogens

AuthorsArolas, Joan L. ; Goulas, Theodoros ; Cuppari, Anna ; Gomis-Rüth, F. Xavier
Issue Date13-Jun-2018
PublisherAmerican Chemical Society
CitationChemical Reviews - Columbus 118(11): 5581–5597 (2018)
AbstractMetallopeptidases cleave polypeptides bound in the active-site cleft of catalytic domains through a general base/acid mechanism. This involves a solvent molecule bound to a catalytic zinc and general regulation of the mechanism through zymogen-based latency. Sixty reported structures from 11 metallopeptidase families reveal that prosegments, mostly N-terminal of the catalytic domain, block the cleft regardless of their size. Prosegments may be peptides (5−14 residues), which are only structured within the zymogens, or large moieties (<227 residues) of one or two folded domains. While some prosegments globally shield the catalytic domain through a few contacts, others specifically run across the cleft in the same or opposite direction as a substrate, making numerous interactions. Some prosegments block the zinc by replacing the solvent with particular side chains, while others use terminal α-amino or carboxylate groups. Overall, metallopeptidase zymogens employ disparate mechanisms that diverge even within families, which supports that latency is less conserved than catalysis
Publisher version (URL)http://dx.doi.org/10.1021/acs.chemrev.8b00030
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