title: Families of metalloendopeptidases and their relationships.
abstract: Crystal structures available for four metalloendopeptidases have revealed zinc ligands for these enzymes. New sequence information has made it possible to compare the primary structures of the zinc-binding site in metalloendopeptidases. A scheme based on the zinc-binding site is proposed to classify metalloendopeptidases into five distinct families: thermolysin, astacin, serratia, matrixin, and snake venom metalloproteinases. Two histidines and one glutamate are zinc-ligands in the thermolysin family. Three histidines and one tyrosine are zinc ligands in the other four families, which are further distinguished by the identity of the residue following the third histidine and by the environment surrounding the tyrosine.
authors.affiliation: Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061.
authors.forename: W
authors.initials: W
authors.lastname: Jiang
authors.forename: J S
authors.initials: JS
authors.lastname: Bond
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D015032:Zinc / Q000378:metabolism
chemical_list: D008666:Metalloendopeptidases; D015032:Zinc