{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T11:43:09Z","timestamp":1791546189693,"version":"4.3.4"},"reference-count":136,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":4993,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1995,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The three\u2010dimensional structures of the zinc endopeptidases human neutrophil collagenase, adamalysin II from rattle snake venom, alkaline proteinase from\n                    <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                    , and astacin from crayfish are topologically similar, with respect to a five\u2010stranded \u03b2\u2010sheet and three \u03b1\u2010helices arranged in typical sequential order. The four proteins exhibit the characteristic consensus motif HEXXHXXGXXH, whose three histidine residues are involved in binding of the catalytically essential zinc ion. Moreover, they all share a conserved methionine residue beneath the active site metal as part of a superimposable \u201cMet\u2010turn.\u201d This structural relationship is supported by a sequence alignment performed on the basis of topological equivalence showing faint but distinct sequential similarity. The alkaline proteinase is about equally distant (26% sequence identity) to both human neutrophil collagenase and astacin and a little further away from adamalysin II (17% identity). The pairs astacin\/adamalysin II, astacin\/human neutrophil collagenase, and adamalysin II\/human neutrophil collagenase exhibit sequence identities of 16%, 14%, and 13%, respectively. Therefore, the corresponding four distinct families of zinc peptidases, the astacins, the matrix metalloproteinases (matrixins, collagenases), the adamalysins\/reprolysins (snake venom proteinases\/reproductive tract proteins), and the serralysins (large bacterial proteases from\n                    <jats:italic>Serratia, Erwinia<\/jats:italic>\n                    , and\n                    <jats:italic>Pseudomonas<\/jats:italic>\n                    ) appear to have originated by divergent evolution from a common ancestor and form a superfamily of proteolytic enzymes for which the designation \u201cmetzincins\u201d has been proposed. There is also a faint but significant structural relationship of the metzincins to the thermolysin\u2010like enzymes, which share the truncated zinc\u2010binding motif HEXXH and, moreover, similar topologies in their N\u2010terminal domains.\n                  <\/jats:p>","DOI":"10.1002\/pro.5560040502","type":"journal-article","created":{"date-parts":[[2010,6,29]],"date-time":"2010-06-29T04:45:56Z","timestamp":1277786756000},"page":"823-840","source":"Crossref","is-referenced-by-count":624,"title":["The metzincins \u2014 Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc\u2010peptidases"],"prefix":"10.1002","volume":"4","author":[{"given":"Walter","family":"St\u00f6cker","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank","family":"Grams","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"Reinemer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfram","family":"Bode","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Baumann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Franz\u2010Xaver","family":"Gomis\u2010R\u00fcth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David B.","family":"Mckay","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(89)90350-0"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1988.tb14220.x"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/348699a0"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1994.1576"},{"key":"e_1_2_1_6_1","first-page":"3357","article-title":"Three\u2010dimensional X\u2010ray crystallographic structure of the alkaline protease of","volume":"12","author":"Baumann U","year":"1993","journal-title":"Pseudomonas aeruginosa. 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