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
Exoerythrocytic Plasmodium Parasites Secrete a Cysteine Protease Inhibitor Involved in Sporozoite Invasion and Capable of Blocking Cell Death of Host Hepatocytes
Annika Rennenberg,Christine Lehmann,Anna Heitmann,Tina Witt,Guido Hansen,Krishna Nagarajan,Christina Deschermeier,Vito Turk,Rolf Hilgenfeld,Volker Heussler +9 more
TL;DR: It is suggested that the inhibitor plays an important role in sporozoite invasion of host cells and in parasite survival during liver stage development by inhibiting host cell proteases involved in programmed cell death.
Journal ArticleDOI
Purification and functional studies of a potent modified quorum-sensing peptide and a two-peptide bacteriocin in Streptococcus mutans.
TL;DR: The findings support the involvement of the CSP response in bacteriocin production by streptococci and suggest a novel strategy to potentiate autoinducer activity.
Journal ArticleDOI
Impact of Insulin Degrading Enzyme and Neprilysin in Alzheimer's Disease Biology: Characterization of Putative Cognates for Therapeutic Applications.
Niraj Kumar Jha,Saurabh Kumar Jha,Dhiraj Kumar,Noopur Kejriwal,Renu Sharma,Rashmi K. Ambasta,Pravir Kumar,Pravir Kumar +7 more
TL;DR: In silico sequential and structural analysis of IDE and NEP has been performed to identify the molecular entities for proteolytic degradation of Aβ in the AD brain, to analyze their catalytic site to demonstrate the enzymatic action played by IDE andNEP.
Journal ArticleDOI
Structural Insight into the Bacterial Mucinase StcE Essential to Adhesion and Immune Evasion during Enterohemorrhagic E. coli Infection
TL;DR: The structure of StcE is determined and a dynamic, multidomain architecture featuring an unusually large substrate-binding cleft and a prominent polarized surface charge distribution highly suggestive of an electrostatic role in substrate targeting is revealed.
Journal ArticleDOI
Comparative structural analysis of the caspase family with other clan CD cysteine peptidases.
Karen McLuskey,Jeremy C. Mottram +1 more
TL;DR: A diverse group of structures with highly conserved structural elements that provide the peptidases with a variety of substrate specificities and activation mechanisms are revealed, suggesting that the metacaspases are structurally diverse from the caspases (and paracaspase), suggesting that they should form a distinct family of clan CD peptidase.
References
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