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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Affinity of Avr2 for tomato cysteine protease Rcr3 correlates with the Avr2-triggered Cf-2-mediated hypersensitive response.
John W. van't Klooster,Marc W. van der Kamp,Jacques Vervoort,Jules Beekwilder,Sjef Boeren,Matthieu H. A. J. Joosten,Bart P. H. J. Thomma,Pierre J. G. M. de Wit +7 more
TL;DR: It is found that the two C-terminal cysteine residues and the six amino acid C-Terminal tail of Avr2 are required for both Rcr3 inhibitory activity and the ability to trigger a Cf-2-mediated HR in tomato.
Journal ArticleDOI
Role of two cysteine proteinases in the susceptible response of Nicotiana benthamiana to Colletotrichum destructivum and the hypersensitive response to Pseudomonas syringae pv. tomato
TL;DR: Two cysteine proteinase genes of the papain family were amplified from cDNA of Nicotiana benthamiana leaves infected with the hemibiotrophic fungus Colletotrichum destructivum and showed peak expression corresponding with the switch from biotrophic to necrotrophic growth by C.destructivum.
Journal ArticleDOI
The molecular analysis of Trypanosoma cruzi metallocarboxypeptidase 1 provides insight into fold and substrate specificity
Gabriela T. Niemirowicz,Daniel Fernández,Maria Solà,Juan José Cazzulo,Francesc X. Avilés,F. Xavier Gomis-Rüth +5 more
TL;DR: The structure of TcMCP‐1 shows strong topological similarity with archaeal, bacterial and mammalian metallopeptidases including angiotensin‐converting enzyme, neurolysin and thimet oligopePTidase.
Journal ArticleDOI
Peptidomic Analysis of Urine from Youths with Early Type 1 Diabetes Reveals Novel Bioactivity of Uromodulin Peptides In Vitro
Julie Anh Dung Van,Julie Anh Dung Van,Sergi Clotet-Freixas,Joyce Zhou,Ihor Batruch,Chunxiang Sun,Michael Glogauer,Luca Rampoldi,Yesmino Elia,Farid H. Mahmud,Etienne Sochett,Eleftherios P. Diamandis,Eleftherios P. Diamandis,James W. Scholey,James W. Scholey,Ana Konvalinka,Ana Konvalinka +16 more
TL;DR: A urinary signature of uromodulin peptides associated with early type 1 diabetes before clinical manifestations of kidney disease is identified and novel bioactivity of two peptides in vitro is demonstrated in vitro using NFκB luciferase activity and neutrophil chemotaxis assays.
Journal ArticleDOI
NtCP56, a new cysteine protease in Nicotiana tabacum L., involved in pollen grain development
TL;DR: It is reported that a new cysteine protease, NtCP56, is involved in the development of pollen grains in Nicotiana tabacum L, and may play an important role in pollen development.
References
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