Families of zinc metalloproteases

  title={Families of zinc metalloproteases},
  author={Nigel M. Hooper},
  journal={FEBS Letters},
  • N. Hooper
  • Published 31 October 1994
  • Biology, Chemistry
  • FEBS Letters

Catalytic Domain Architecture of Metzincin Metalloproteases*

  • F. Gomis-Rüth
  • Biology, Chemistry
    The Journal of Biological Chemistry
  • 2009
Seven metzincins families are subdivided into families, and seven such families have been analyzed at the structural level: the astacins, ADAMs/adamalysins/reprolysins, serralysins, matrix metalloproteinases, snapalysins, leishmanolysins, and pappalysins.

Identification of Glutamate Residues Essential for Catalytic Activity and Zinc Coordination in Aminopeptidase A (*)

Results provide evidence that Glu-408 is the third zinc-coordinating residue of APA, confirm the presumed involvement of GLU-386 in the catalytic process of the enzyme, and identify APA as a zinc metallopeptidase functionally similar to thermolysin.

Structural features of a superfamily of zinc-endopeptidases: the metzincins.

Aspzincin, a Family of Metalloendopeptidases with a New Zinc-binding Motif

Deuterolysin (EC; formerly designated as neutral proteinase II) from Aspergillus oryzae, which contains 1 g atom of zinc/mol of enzyme, is a single chain of 177 amino acid residues,

Structural aspects of the metzincin clan of metalloendopeptidases

This clan is reviewed from a structural point of view, based on the reported structures of representative members of the astacins, adamalysins, serralysins, matrixins, snapalysin, and leishmanolysins, and of inhibited forms, either by specific endogenous protein inhibitors or by zymogenic pro-domains.

CLCAs - A Family of Metalloproteases of Intriguing Phylogenetic Distribution and with Cases of Substituted Catalytic Sites

An extremely patchy phylogenetic distribution of CLCAs in prokaryotes and their conserved protein domain composition strongly suggests an evolutionary scenario of horizontal gene transfer (HGT) from multicellular eukaryotes to bacteria, providing an example of eUKaryote-derived xenologues in bacterial genomes.

The metzincin-superfamily of zinc-peptidases.

The three-dimensional structures of a number of zinc proteinases that share the zinc-binding motif HEXXHXXGXXH have been elucidated and represent four different families of zinc peptidases: the astacins, adamalysin II, bacterial serralysins, and the matrixins (matrix metalloproteinases, MMPs).

Architecture and function of metallopeptidase catalytic domains

Accumulated structural data from more than 300 deposited structures of the 12 currently characterized metzincin families provide detailed knowledge of the molecular features of their catalytic domains, help in the understanding of their working mechanisms, and form the basis for the design of novel drugs.



Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes.

A novel active site has been identified in a family of zinc-dependent metalloendopeptidases that includes bacterial proteinase III, the human and Drosophila insulin-degrading enzymes, and the

Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis.

The combined loss of enzyme activities and zinc content in the purified mutated mouse proteins, emphasizes the critical role of the zinc atom for catalysis, whereas the virtually identical chromatographic behaviors of the mutated and nonmutated mouse LTA4 hydrolase proteins suggest that the metal is of limited importance for the maintenance of the enzyme tertiary structure.

Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11.

The changes made to Asp650 of NEP by site-directed mutagenesis and expressed the mutant enzymes in COS-1 cells strongly support the conclusion that Asp 650 in NEP is crucial for hydrolytic activity.

First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases.

The snake venom metalloproteinases and the astacins might be grouped into a common superfamily with distinct differences from the thermolysin family, due to their virtually identical active‐site environment and similar folding topology.

Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution

The structure of the penicillin-resistant Zn2+-containing D-alanyl-D-alanine peptidase of Streptomyces albus and the mechanism of action of the enzyme may be related to that of other carboxypeptidases, which also contain functional Zn 2+ ions.