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
High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation.
Eva Zerovnik,Katja Skerget,Magda Tusek-Znidaric,Corina Loeschner,Marcus W. Brazier,David R. Brown +5 more
TL;DR: It is shown that human stefin’B, a protease inhibitor from the family of cystatins, is a copper binding protein, unlike stefIn’A, and that copper binding inhibits the amyloid fibril formation and, to a lesser degree, the initial aggregation.
Journal ArticleDOI
Peptidomics analysis of human blood specimens for biomarker discovery
TL;DR: This review addresses the concepts, limitations and perspectives for the application of peptidomics science and technologies to discover putative biomarkers in blood specimens.
Journal ArticleDOI
Genetic Analysis of 15 Protein Folding Factors and Proteases of the Escherichia coli Cell Envelope
Juliane Weski,Michael Ehrmann +1 more
TL;DR: The physiological implications of 15 factors of the E. coli cell envelope are determined by an integrated genetic approach comprising phenotypic analyses and it is shown that in degP dsbA, degP tsp, and degP yfgC double mutants a subpopulation of LamB exists as unfolded monomers.
Journal ArticleDOI
Metabolome and proteome changes between biofilm and planktonic phenotypes of the marine bacterium Pseudoalteromonas lipolytica TC8.
Laurie Favre,Annick Ortalo-Magné,Carole Pichereaux,Carole Pichereaux,Audrey Gargaros,Odile Burlet-Schiltz,Valérie Cotelle,Gérald Culioli +7 more
TL;DR: Differences between proteomes revealed that peptidases, oxidases, transcription factors, membrane proteins and the enzymes involved in histidine biosynthesis were over-expressed in biofilms while proteins involved in heme production, nutrient assimilation, cell division and arginine/ornithine biosynthetic were specifically up-regulated in free-living cells.
Journal ArticleDOI
Activity‐based mass spectrometric characterization of proteases and inhibitors in human saliva
TL;DR: Regulation of oral fluid proteolysis is highly important given that an inbalance in such activities has been correlated to a variety of pathological conditions including oral cancer.
References
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