title: Structural features of a superfamily of zinc-endopeptidases: the metzincins.
abstract: A large number of zinc endopeptidases contain an HEXXHXXGXXH consensus motif in their catalytic site (single letter code; X is any amino acid residue). These enzymes can be grouped into four distinct families, the astacins, the adamalysins, the serralysins and the matrix metalloproteinases (matrixins). Despite a low degree of sequence similarity, their catalytic modules are topologically similar. A topology derived sequence alignment suggests that the four families form a superfamily, called the metzincins because of a perfectly superimposable methionine residue close to the zinc-binding active site. Topological similarity to the thermolysin-like enzymes indicates that these enzymes may have had a common ancestor.
authors.affiliation: Zoologisches Institut der Universität Heidelberg, Germany.
authors.forename: W
authors.initials: W
authors.lastname: Stöcker
authors.forename: W
authors.initials: W
authors.lastname: Bode
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000145:classification; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D017421:Sequence Analysis; D015032:Zinc / Q000737:chemistry*
chemical_list: D008666:Metalloendopeptidases; D015032:Zinc