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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Characterization of a New S8 serine Protease from Marine Sedimentary Photobacterium sp. A5-7 and the Function of Its Protease-Associated Domain.
Hui-Juan Li,Bai-Lu Tang,Xuan Shao,Bai-Xue Liu,Xiao-Yu Zheng,Xiao-Xu Han,Ping-Yi Li,Xi-Ying Zhang,Xiao-Yan Song,Xiu-Lan Chen +9 more
TL;DR: Direct evidence that the PA domain of a subtilase can bind substrate is shown, which provides a better understanding of the function of the PAdomain of subtilases and bacterial extracellular proteases from marine sediment.
Journal ArticleDOI
The structure and specificity of the type III secretion system effector NleC suggest a DNA mimicry mechanism of substrate recognition.
TL;DR: NleC is investigated as a zinc protease that cleaves NF-κB transcription factors and displays a modified Ψ-loop motif that may be important for folding and refolding requirements implicit in T3SS translocation, and is a member of the Zincin protease superfamily, albeit divergent from its structural homologues.
Journal ArticleDOI
Optimization and Immobilization of Purified Labeo rohita Visceral Protease by Entrapment Method.
S. Geethanjali,Anitha Subash +1 more
TL;DR: The purified fish visceral protease enzyme was immobilized by using various concentrations of sodium alginate and calcium chloride to optimize the best concentration for the formation of spherical and stable beads and was characterized by assaying the optimal pH, temperature, storage stability and reusability.
Journal ArticleDOI
The multifaceted roles of tumor-associated proteases and harnessing their activity for prodrug activation.
TL;DR: Some of the advances in understanding of the roles of several key proteases from different classes in the development and progression of cancer and the potential to leverage their upregulated activity for the development of novel targeted treatment strategies are discussed.
Journal ArticleDOI
Stage-specific expression of protease genes in the apicomplexan parasite, Eimeria tenella
Marilyn Katrib,Rowan J. Ikin,Fabien Brossier,Michelle Robinson,Iveta Slapetova,Philippa A Sharman,Robert A. Walker,Sabina I. Belli,Fiona M. Tomley,Nicholas Smith +9 more
TL;DR: Eimeria tenella possesses a large number of protease genes that appear to be unique to the Coccidia and may play key roles in the formation of the oocyst wall, a defining feature of this group of parasites.
References
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