{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,6,23]],"date-time":"2025-06-23T07:28:04Z","timestamp":1750663684598},"reference-count":48,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2008,6,28]],"date-time":"2008-06-28T00:00:00Z","timestamp":1214611200000},"content-version":"vor","delay-in-days":11136,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1978,1]]},"abstract":"<jats:p>Two new enzymes, which catalyze the synthesis of stizolobinic acid and stizolobic acid through oxidative ring cleavage of 3,4\u2010dihydroxyphenylalanine, subsequent recyclization and dehydrogenation of the resultant possible products were isolated from the soluble protein extract of <jats:italic>Stizolobium hassjoo<\/jats:italic> seedlings and were purified approximately 100\u2010fold by ammonium sulfate fractionation followed by column chromatography on Sephadex G\u2010100, DEAE\u2010cellulose and hydroxyapatite. The apparent molecular weights of both enzymes as determined by Sephadex G\u2010100 column chromatography were 45 000. The pH optima were 7.6 and 7.4, apparent <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> values for 3,4\u2010dihydroxyphenylalanine as substrate were 1.67 mM and 1.39 mM for the enzymes to synthesize stizolobinic acid and stizolobic acid, respectively. Both enzymes required NADP<jats:sup>+<\/jats:sup> for the activities. They were activated by Zn<jats:sup>2+<\/jats:sup> and inhibited by sulfhydryl binding and zinc chelating agents. Both exhibited a strict specificity for 3,4\u2010dihydroxyphenylalanine as substrate and showed no affinities for other <jats:italic>o<\/jats:italic>\u2010dihydric phenols tested. The enzymes were very labile with a half\u2010life of 3\u20135 h at 30\u00b0C but they could be stored at \u221220\u00b0C for about 3 months under nitrogen gas with 0.1 mM dithiothreitol without appreciable loss of the catalytic enzyme activities.<\/jats:p><jats:p>These enzymes have never been reported in any biological material. The trivial names, stizolobinic acid synthase and stizolobic acid synthase, are proposed.<\/jats:p>","DOI":"10.1111\/j.1432-1033.1978.tb12033.x","type":"journal-article","created":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T18:27:02Z","timestamp":1109874422000},"page":"385-392","source":"Crossref","is-referenced-by-count":26,"title":["Biosynthesis of Stizolobinic Acid and Stizolobic Acid in Higher Plants"],"prefix":"10.1111","volume":"82","author":[{"given":"Koshi","family":"SAITO","sequence":"first","affiliation":[]},{"given":"Atsushi","family":"KOMAMINE","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2008,6,28]]},"reference":[{"key":"e_1_2_2_2_2","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1515\/znc-1975-9-1017","volume":"30","author":"Saito K.","year":"1975","journal-title":"Z. 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