{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,7]],"date-time":"2026-03-07T13:42:36Z","timestamp":1772890956004,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2003,4,15]]},"abstract":"<jats:p>A proteinase that hydrolyses clupeine and salmine at acidic pH, called aorsin, was found in the fungus Aspergillus oryzae. Purified aorsin also hydrolysed benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide optimally at pH4.0. The specificity of aorsin appeared to require a basic residue at the P1 position and to prefer paired basic residues. Aorsin activated plasminogen and converted trypsinogen to trypsin. The trypsin-like activity was inhibited strongly by antipain or leupeptin, but was not inhibited by any other standard inhibitors of peptidases. To identify the catalytic residues of aorsin, a gene was cloned and an expression system was established. The predicted mature protein of aorsin was 35% identical with the classical late-infantile neuronal ceroid lipofuscinosis protein CLN2p and was 24% identical with Pseudomonas serine-carboxyl proteinase, both of which are pepstatin-insensitive carboxyl proteinases. Several putative catalytic residues were mutated. The kcat\/Km values of the mutant enzymes Glu86\u2192Gln, Asp211\u2192Asn and Ser354\u2192Thr were 3\u20134 orders of magnitude lower and Asp90\u2192Asn was 21-fold lower than that of wild-type aorsin, indicating that the positions are important for catalysis. Aorsin is another of the S53 family serine-carboxyl proteinases that are not inhibited by pepstatin.<\/jats:p>","DOI":"10.1042\/bj20021691","type":"journal-article","created":{"date-parts":[[2003,4,9]],"date-time":"2003-04-09T09:34:54Z","timestamp":1049880894000},"page":"541-548","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Aorsin, a novel serine proteinase with trypsin-like specificity at acidic pH"],"prefix":"10.1042","volume":"371","author":[{"given":"Byung Rho","family":"LEE","sequence":"first","affiliation":[{"name":"Laboratory of Molecular Enzymology, Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masato","family":"FURUKAWA","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Enzymology, Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Koichiro","family":"YAMASHITA","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Enzymology, Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yurie","family":"KANASUGI","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Enzymology, Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Choko","family":"KAWABATA","sequence":"additional","affiliation":[{"name":"Technical Research Center of T. Hasegawa Co., Ltd., Kariyado, 335 Nakahara-ku, Kawasaki 211-0022, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kenichi","family":"HIRANO","sequence":"additional","affiliation":[{"name":"Gifu R and D Center of Amano Enzyme Inc., 4-179-35, Sue-cho, Kakamigahara, Gifu 509-0108, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kenichi","family":"ANDO","sequence":"additional","affiliation":[{"name":"Gifu R and D Center of Amano Enzyme Inc., 4-179-35, Sue-cho, Kakamigahara, Gifu 509-0108, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eiji","family":"ICHISHIMA","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Enzymology, Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan"},{"name":"Laboratory of Molecular Enzymology, Division of Bioengineering, Graduate School of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/371\/2\/541\/711059\/bj3710541.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/371\/2\/541\/711059\/bj3710541.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T12:39:05Z","timestamp":1637584745000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/371\/2\/541\/40793\/Aorsin-a-novel-serine-proteinase-with-trypsin-like"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,4,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2003,4,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20021691","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2003,4,15]]}}}