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
The mechanism of inhibition of antibody-based inhibitors of membrane-type serine protease 1 (MT-SP1).
TL;DR: The mechanisms of inhibition of two novel scFv antibody inhibitors of the serine protease MT-SP1/matriptase are revealed and suggest that the development of specific antibody-based inhibitors against individual members of closely related enzyme families is feasible, and an effective way to develop tools to tease apart complex biological processes.
Journal ArticleDOI
Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).
Qing-Na Cao,Marlene Stubbs,Kenny Q.P. Ngo,Michael Ward,Annie Cunningham,Emil F. Pai,Guang-Chou Tu,Theo Hofmann +7 more
TL;DR: The results show that the putative hydrogen bond alone is responsible for the increase in penicillopepsin‐JT2, and it is proposed that by locking the ‐NH‐ of P3 to the enzyme, the scissile peptide bond between P1 and P1′ becomes distorted toward a tetrahedral conformation and becomes more susceptible to nucleophilic attack by the catalytic apparatus without the need of a conformational change in the enzyme.
Journal ArticleDOI
Septic injury-inducible genes in medicinal maggots of the green blow fly Lucilia sericata.
TL;DR: The suppression subtractive hybridization method was used to screen for genes that are differentially expressed in response to septic wounding of sterile second instar larvae of L. sericata, resulting in the identification of 65 novel Lucilia genes including potential signalling proteins and a number of digestive enzymes including lipases and proteinases.
Book ChapterDOI
Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furin.
Ujwal Shinde,Gary Thomas +1 more
TL;DR: This chapter review what has learned from the folding and activation of prokaryotic subtilisin, discuss how this has molded the authors' understanding of furin maturation, and foray into the concept of pH sensors, which may represent a paradigm that PCs (and possibly other IMC-dependent eukaryotic proteins) follow for regulating their biological functions using the pH gradient in the secretory pathway.
Journal ArticleDOI
Antioxidant, angiotensin-converting enzyme inhibitory activity and other functional properties of egg white proteins and their derived peptides - A review.
TL;DR: These peptides are known for their beneficial activities in vitro only, and little work has been done to prove their beneficial effects in vivo, therefore, further studies are needed to see if the bioactive peptides derived from egg white proteins are helpful for humans in the future.
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