Peptidases (often termed proteases) are of great relevance to biology, medi
cine, and biotechnology. This practical importance creates a need for an in
tegrated source of information about peptidases. In the MEROPS database (ww
w.merops.ac.uk), peptidases are classified by structural similarities in th
e parts of the molecules responsible for their enzymatic activity. They are
grouped into families on the basis of amino acid sequence homology, and th
e families are assembled into clans in light of evidence that they share co
mmon ancestry. The evidence for clan-level relationships usually comes from
similarities in tertiary structure, but we suggest that secondary structur
e profiles may also be useful in the future. The classification forms a fra
mework around which a wealth of supplementary information about the peptida
ses is organized. This includes images of three-dimensional structures, ali
gnments of matching human and mouse ESTs, comments on biomedical relevance,
human and other gene symbols, and literature references linked to PubMed.
For each family, there is an amino acid sequence alignment and a dendrogram
. There is a list of all peptidases known from each of over 1000 species, t
ogether with summary data for the distributions of the families and clans t
hroughout the major groups of organisms. A set of online searches provides
access to information about the location of peptidases on human chromosomes
and peptidase substrate specificity. (C) 2001 Academic Press.