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
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Journal ArticleDOI
Bovine Meat Proteins as Potential Precursors of Biologically Active Peptides – a Computational Study based on the BIOPEP Database
TL;DR: Among the examined proteins, collagen and elastin appear to be the richest potential source of bioactive peptides, in particular of angiotensin-converting enzyme inhibitors, antithrombotic fragments, inhibitors of dipeptidyl peptidase IV and peptides regulating gastric mucosal activity.
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Mutations in LRPAP1 are associated with severe myopia in humans.
Mohammed A. Aldahmesh,Arif O. Khan,Hisham Alkuraya,Nouran Adly,Shamsa Anazi,Ahmed A. Al-Saleh,Jawahir Y. Mohamed,Hadia Hijazi,Sarita Prabakaran,Marlene Tacke,Abdullah Al-Khrashi,Mais Hashem,Thomas Reinheckel,Abdullah Mohammed Assiri,Fowzan S. Alkuraya +14 more
TL;DR: Mendelian forms of myopia in four consanguineous families are identified and exome/autozygome analysis is implemented to identify homozygous truncating variants in LRPAP1 and CTSH as the likely causal mutations.
Journal ArticleDOI
Slicing a protease: Structural features of the ATP‐dependent Lon proteases gleaned from investigations of isolated domains
T. V. Rotanova,Istvan Botos,E.E. Melnikov,Fatima Rasulova,Alla Gustchina,Michael R. Maurizi,Alexander Wlodawer +6 more
TL;DR: The structure of a large segment of the N‐terminal domain has revealed a folding motif present in other protein families of unknown function and should lead to new insights regarding ways in which Lon interacts with substrates or other cellular factors.
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Structure-based dissection of the active site chemistry of leukotriene a4 hydrolase: implications for m1 aminopeptidases and inhibitor design.
Fredrik Tholander,Ayumo Muroya,Bernard-Pierre Roques,Marie-Claude Fournie-Zaluski,Marjolein M. G. M. Thunnissen,Jesper Z. Haeggström +5 more
TL;DR: This work shows that peptide turnover by the M1 prototype, leukotriene A4 hydrolase/aminopeptidase, involves a shift in substrate position associated with exchange of zinc coordinating groups, while maintaining the overall coordination geometry.
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Proteolytic Activity Matrix Analysis (PrAMA) for Simultaneous Determination of Multiple Protease Activities
Miles A. Miller,Layla J. Barkal,Karen Jeng,Andreas Herrlich,Marcia L. Moss,Linda G. Griffith,Douglas A. Lauffenburger +6 more
TL;DR: Results indicate PrAMA can distinguish closely related enzymes from each other with high accuracy, even in the presence of unknown background proteolytic activity, and offers a valuable tool for applications ranging from live-cell in vitro assays to high-throughput inhibitor screening with complex enzyme mixtures.
References
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