{"title":"二价金属离子对葡萄糖基转移酶的亚位点特异性。","authors":"K S Devulapalle, G Mooser","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Glucosyltransferase from oral bacteria Streptococcus mutans is the most significant virulent factor in causing dental caries. The enzyme has two subsites. The binding specificity of divalent metal ions to glucosyl or fructosyl subsite was examined using multiple inhibition kinetics. The interaction factor \"alpha\" identifies whether the two subsites are exclusive or non-exclusive.</p>","PeriodicalId":77201,"journal":{"name":"Journal of craniofacial genetics and developmental biology","volume":"20 2","pages":"107-8"},"PeriodicalIF":0.0000,"publicationDate":"2000-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Subsite specificity of divalent metal ions to glucosyltransferase.\",\"authors\":\"K S Devulapalle, G Mooser\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Glucosyltransferase from oral bacteria Streptococcus mutans is the most significant virulent factor in causing dental caries. The enzyme has two subsites. The binding specificity of divalent metal ions to glucosyl or fructosyl subsite was examined using multiple inhibition kinetics. The interaction factor \\\"alpha\\\" identifies whether the two subsites are exclusive or non-exclusive.</p>\",\"PeriodicalId\":77201,\"journal\":{\"name\":\"Journal of craniofacial genetics and developmental biology\",\"volume\":\"20 2\",\"pages\":\"107-8\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-04-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of craniofacial genetics and developmental biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of craniofacial genetics and developmental biology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Subsite specificity of divalent metal ions to glucosyltransferase.
Glucosyltransferase from oral bacteria Streptococcus mutans is the most significant virulent factor in causing dental caries. The enzyme has two subsites. The binding specificity of divalent metal ions to glucosyl or fructosyl subsite was examined using multiple inhibition kinetics. The interaction factor "alpha" identifies whether the two subsites are exclusive or non-exclusive.
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