
Peptidases, their substrates and inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfil the need for an integrated source of information about these. The database has a hierarchical classification in which homologous sets of peptidases and protein inhibitors are grouped into protein species, which are grouped into families, which are in turn grouped into clans. The classification framework is used for attaching information at each level. An important focus of the database has become distinguishing one peptidase from another through identifying the specificity of the peptidase in terms of where it will cleave substrates and with which inhibitors it will interact. We have collected over 39,000 known cleavage sites in proteins, peptides and synthetic substrates. These allow us to display peptidase specificity and alignments of protein substrates to give an indication of how well a cleavage site is conserved, and thus its probable physiological relevance. While the number of new peptidase families and clans has only grown slowly the number of complete genomes has greatly increased. This has allowed us to add an analysis tool to the relevant species pages to show significant gains and losses of peptidase genes relative to related species.
Internet, Sequence Homology, Amino Acid, Archaeal Proteins, Molecular Sequence Data, Computational Biology, Information Storage and Retrieval, Articles, Genome, Viral, Genomics, Protein Structure, Tertiary, Databases, Genetic, Animals, Humans, Amino Acid Sequence, Databases, Protein, Software, Peptide Hydrolases
Internet, Sequence Homology, Amino Acid, Archaeal Proteins, Molecular Sequence Data, Computational Biology, Information Storage and Retrieval, Articles, Genome, Viral, Genomics, Protein Structure, Tertiary, Databases, Genetic, Animals, Humans, Amino Acid Sequence, Databases, Protein, Software, Peptide Hydrolases
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