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
Molecular and biological screening for insect-toxic seed albumins from four legume species
Sandrine Louis,Bernard Delobel,Frédéric Gressent,Isabelle Rahioui,Laurence Quillien,Agnès Vallier,Yvan Rahbé +6 more
TL;DR: By using a combination of molecular, biochemical and specific insect bioassays, new genes and their products from the seeds of four legume species are characterised, indicating possible variant post-translational processing of A1b within legumes.
Journal ArticleDOI
An alternative view of the proposed alternative activities of hemopexin
TL;DR: An homology model of the three‐dimensional structure of human hemopexin is used to reveal that the protein lacks the catalytic triad that is characteristic of many serine proteases but that hemopxin possesses two highly exposed Arg‐Gly‐Glu sequences that may promote interaction with cell surfaces.
Journal ArticleDOI
Mass spectrometry‐based proteomics strategies for protease cleavage site identification
TL;DR: The present review focuses on mass spectrometry‐based proteomic methods for the analysis of protease cleavage sites, including the identification of the hydrolyzed bonds as well as of the surrounding sequence.
Journal ArticleDOI
Anti-staphylococcal activities of lysostaphin and LytM catalytic domain
Izabela Sabala,Izabela Sabala,Ing-Marie Jonsson,Andrej Tarkowski,Matthias Bochtler,Matthias Bochtler,Matthias Bochtler +6 more
TL;DR: Although lysostaphin and LytM cleave the same peptide bond in the peptidoglycan, the two enzymes have very different environmental requirements what is reflected in their contrasting performance in mouse eczema model.
Journal ArticleDOI
An in vitro selection strategy for conferring protease resistance to ligand binding peptides
Bill Eldridge,R. Neil Cooley,Richard Odegrip,Duncan Mcgregor,Kevin Fitzgerald,Christopher Ullman +5 more
TL;DR: In vitro display technology, CIS display, is used to enhance the proteolytic resistance of ligand-binding peptides by selection of protecting motifs from a large peptide library, which translated into increased resistance to plasma proteases in vitro and to an increase in circulating half-lives in rats.
References
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