{"title":"D-和l -6-羟尼古丁氧化酶，氧化节杆菌的对映酶。","authors":"K Decker, V D Dai, H Möhler, M Brühmüller","doi":"10.1515/znb-1972-0921","DOIUrl":null,"url":null,"abstract":"D- and ʟ-hydroxynicotine oxidase were obtained in homogeneous form and compared with regard to molecular weight, subunit structure, reaction mechanism, and specificity. The most striking differences between these enantiozymes are the type of coenzyme binding and the reactivity towards artificial two-electron acceptors.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 9","pages":"1072-3"},"PeriodicalIF":0.0000,"publicationDate":"1972-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0921","citationCount":"8","resultStr":"{\"title\":\"D- and L-6-hydroxynicotine oxidase, enantiozymes of Arthrobacter oxidans.\",\"authors\":\"K Decker, V D Dai, H Möhler, M Brühmüller\",\"doi\":\"10.1515/znb-1972-0921\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"D- and ʟ-hydroxynicotine oxidase were obtained in homogeneous form and compared with regard to molecular weight, subunit structure, reaction mechanism, and specificity. The most striking differences between these enantiozymes are the type of coenzyme binding and the reactivity towards artificial two-electron acceptors.\",\"PeriodicalId\":78857,\"journal\":{\"name\":\"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie\",\"volume\":\"27 9\",\"pages\":\"1072-3\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1972-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/znb-1972-0921\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/znb-1972-0921\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/znb-1972-0921","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
D- and L-6-hydroxynicotine oxidase, enantiozymes of Arthrobacter oxidans.
D- and ʟ-hydroxynicotine oxidase were obtained in homogeneous form and compared with regard to molecular weight, subunit structure, reaction mechanism, and specificity. The most striking differences between these enantiozymes are the type of coenzyme binding and the reactivity towards artificial two-electron acceptors.
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