{"title":"d -氨基酸氧化酶与-氯丙氨酸反应的停流动力学与稳态动力学比较。","authors":"J G Voet, D J Porter, H J Bright","doi":"10.1515/znb-1972-0915","DOIUrl":null,"url":null,"abstract":"We describe anaerobic stopped-flow monitored interactions of D-B-chloroalanine with D-amino acid oxidase and show that the kinetics of absorbance changes at 550 nm due to enzyme-bound intermediates can not be correlated with steady state turnover behavior unless it is assumed that only a small fraction of the enzyme directly participates in the α-β elimination process.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 9","pages":"1054-5"},"PeriodicalIF":0.0000,"publicationDate":"1972-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0915","citationCount":"3","resultStr":"{\"title\":\"Comparison of stopped flow and steady state kinetics in the reaction of D-amino-acid oxidase with -chloroalanine.\",\"authors\":\"J G Voet, D J Porter, H J Bright\",\"doi\":\"10.1515/znb-1972-0915\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"We describe anaerobic stopped-flow monitored interactions of D-B-chloroalanine with D-amino acid oxidase and show that the kinetics of absorbance changes at 550 nm due to enzyme-bound intermediates can not be correlated with steady state turnover behavior unless it is assumed that only a small fraction of the enzyme directly participates in the α-β elimination process.\",\"PeriodicalId\":78857,\"journal\":{\"name\":\"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie\",\"volume\":\"27 9\",\"pages\":\"1054-5\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1972-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/znb-1972-0915\",\"citationCount\":\"3\",\"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-1972-0915\",\"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-1972-0915","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Comparison of stopped flow and steady state kinetics in the reaction of D-amino-acid oxidase with -chloroalanine.
We describe anaerobic stopped-flow monitored interactions of D-B-chloroalanine with D-amino acid oxidase and show that the kinetics of absorbance changes at 550 nm due to enzyme-bound intermediates can not be correlated with steady state turnover behavior unless it is assumed that only a small fraction of the enzyme directly participates in the α-β elimination process.