MEROPS: the peptidase database
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TLDR
The MEROPS database has added an analysis tool to the relevant species pages to show significant gains and losses of peptidase genes relative to related species, and has collected over 39 000 known cleavage sites in proteins, peptides and synthetic substrates.Abstract:
Peptidases (proteolytic enzymes) are of great relevance to biology, medicine and biotechnology. This practical importance creates a need for an integrated source of information about them, and also about their natural inhibitors. The MEROPS database (http://merops.sanger.ac.uk) aims to fill this need. The organizational principle of the database is a hierarchical classification in which homologous sets of the proteins of interest are grouped in families and the homologous families are grouped in clans. Each peptidase, family and clan has a unique identifier. The database has recently been expanded to include the protein inhibitors of peptidases, and these are classified in much the same way as the peptidases. Forms of information recently added include new links to other databases, summary alignments for peptidase clans, displays to show the distribution of peptidases and inhibitors among organisms, substrate cleavage sites and indexes for expressed sequence tag libraries containing peptidases. A new way of making hyperlinks to the database has been devised and a BlastP search of our library of peptidase and inhibitor sequences has been added.read more
Citations
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Journal ArticleDOI
A distinctive repertoire of cathepsins is expressed by juvenile invasive Fasciola hepatica
Martín Cancela,Daniel Acosta,Gabriel Rinaldi,Edileusa Silva,Rosario Durán,Leda Roche,Arnaldo Zaha,Carlos Carmona,José F. Tort +8 more
TL;DR: The existence of a NEJ-specific repertoire of cathepsins expressed early in invasion, distinct to those used by other trematodes, potentially relevant for specific vaccine and chemotherapy design is demonstrated.
Journal ArticleDOI
Approaching the degradome in idiopathic pulmonary fibrosis
TL;DR: Evidence highlights the increasing diversity in both substrates and functions of these enzymes and the complexity of the processes in which they are involved, and indicate a critical role in the abnormal remodeling of IPF.
Journal ArticleDOI
Asparagine Peptide Lyases A SEVENTH CATALYTIC TYPE OF PROTEOLYTIC ENZYMES
TL;DR: Ten families based on sequence similarity in which cleavage is thought to be catalyzed by an asparagine are assembled, defining the seventh proteolytic catalytic type and the first to be discovered since 2004.
Journal ArticleDOI
Isolation and Characterization of Metalloproteases with a Novel Domain Structure by Construction and Screening of Metagenomic Libraries
TL;DR: Sequence and biochemical analyses revealed that MprA and MprB are similar extracellular proteases belonging to the M4 family of metallopeptidases (thermolysin-like family) and that the C-terminal extension is not essential for protease activity.
Journal ArticleDOI
ADAMTS8 and ADAMTS15 expression predicts survival in human breast carcinoma.
Sarah Porter,Paul N. Span,Fred C.G.J. Sweep,V.C.G. Tjan-Heijnen,Caroline J. Pennington,Tanja X. Pedersen,Morten Johnsen,Leif R. Lund,John Rømer,Dylan R. Edwards +9 more
TL;DR: Results observed in FVB‐PyMT mice, a robust transgenic model of highly metastatic breast carcinoma, fitted the expectation that relatively high expression levels of ADAMTS8 together with low expression levels with thrombospondin motifs seen in human breast cancer are associated with a poor clinical outcome.
References
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