Multiple Architectures and Mechanisms of Latency in Metallopeptidase Zymogens

Chemical Reviews
Joan L ArolasF Xavier Gomis-Rüth

Abstract

Metallopeptidases 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.

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Citations

Jan 13, 2019·Applied and Environmental Microbiology·T RochatE Duchaud
Jan 18, 2020·IUCrJ·Evette S Radisky
Mar 31, 2021·Proceedings of the National Academy of Sciences of the United States of America·Ulrich EckhardF Xavier Gomis-Rüth
Mar 28, 2021·Journal of Molecular Biology·Laura Del Amo-MaestroF Xavier Gomis-Rüth
Apr 29, 2021·The Biochemical Journal·D Judy ShonStacy A Malaker
Oct 12, 2021·Frontiers in Microbiology·Alicja WysockaIzabela Sabała

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