{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T05:17:48Z","timestamp":1779340668599,"version":"3.51.4"},"reference-count":31,"publisher":"Wiley","issue":"2-3","license":[{"start":{"date-parts":[[2001,12,17]],"date-time":"2001-12-17T00:00:00Z","timestamp":1008547200000},"content-version":"vor","delay-in-days":3325,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[1992,11,9]]},"abstract":"<jats:p>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\u2010binding site in metalloendopeptidases. A scheme based on the zinc\u2010binding 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\u2010ligands in the thermolysin family. Three histidines and one tyrosine are zinc ligands in other four families, which are further distinguished by the identity of the residue following the third histidine and by the environment surrounding the tyrosine.<\/jats:p>","DOI":"10.1016\/0014-5793(92)80916-5","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T07:42:02Z","timestamp":1027582922000},"page":"110-114","source":"Crossref","is-referenced-by-count":163,"title":["Families of metalloendopeptidases and their relationships"],"prefix":"10.1002","volume":"312","author":[{"given":"Weiping","family":"Jiang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Judith 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