{"title":"塔卡淀粉酶A的结构及其催化意义","authors":"Y. Matsuura, M. Kusunoki, M. Kakudo","doi":"10.5458/JAG1972.38.137","DOIUrl":null,"url":null,"abstract":"Taka-amylase has a (αβ)8 barrel structure and the active site is located at the C-terminal end of a β-strand as reported earlier. In this paper, we describe about the direction of substrate amylose binding with respect to the barrel structure. A possible mechanism of hydrolysis is also proposed, in which Glu 230, Asp 297 and Asp 206 located near the active site are essentially involved.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"33 1","pages":"137-139"},"PeriodicalIF":0.0000,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"13","resultStr":"{\"title\":\"Structure and Catalytic Implications of Taka-Amylase A\",\"authors\":\"Y. Matsuura, M. Kusunoki, M. Kakudo\",\"doi\":\"10.5458/JAG1972.38.137\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Taka-amylase has a (αβ)8 barrel structure and the active site is located at the C-terminal end of a β-strand as reported earlier. In this paper, we describe about the direction of substrate amylose binding with respect to the barrel structure. A possible mechanism of hydrolysis is also proposed, in which Glu 230, Asp 297 and Asp 206 located near the active site are essentially involved.\",\"PeriodicalId\":17372,\"journal\":{\"name\":\"Journal of the Japanese Society of Starch Science\",\"volume\":\"33 1\",\"pages\":\"137-139\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-06-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"13\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of the Japanese Society of Starch Science\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.5458/JAG1972.38.137\",\"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 the Japanese Society of Starch Science","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.5458/JAG1972.38.137","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 13
摘要
taka -淀粉酶具有(αβ)8桶状结构，活性位点位于β链的c端。在本文中，我们描述了相对于桶状结构的底物直链淀粉结合的方向。本文还提出了一种可能的水解机制，其中位于活性位点附近的Glu 230、Asp 297和Asp 206主要参与了水解。
Structure and Catalytic Implications of Taka-Amylase A
Taka-amylase has a (αβ)8 barrel structure and the active site is located at the C-terminal end of a β-strand as reported earlier. In this paper, we describe about the direction of substrate amylose binding with respect to the barrel structure. A possible mechanism of hydrolysis is also proposed, in which Glu 230, Asp 297 and Asp 206 located near the active site are essentially involved.
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