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ENZYME STRUCTURE

ENZYME STRUCTURE
酶结构
批准号：
3917784
负责人：
D R DAVIES
金额：
$0.0万
依托单位：
NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
依托单位国家：
美国
项目类别：
财政年份：
--
资助国家：
美国
项目状态：
未结题
起止时间：
至
来源：
https://reporter.nih.gov/project-details/3917784
关键词：
Salmonella typhimurium X ray crystallography aspartate computer graphics /printing computer simulation cow enzyme inhibitors enzyme mechanism enzyme structure molecular biology peptidases protease inhibitor protein engineering stereochemistry tryptophan synthase

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中文摘要
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英文摘要
1) Additional inhibitor studies on the aspartyl proteinase from Rhizopus chinensis have been carried out. The inhibitors, analogs of pepstatin, provide information regarding the mechanism of action of this class of enzyme and support the concept of rational drug design based on a knowledge of three-dimensional structure. 2) The structure of the enzyme tryptophan synthase from Salmonella typhimurium has been further studied and partially refined. The enzyme, which is bifunctional with an alpha and beta reaction, is organized in an approximately linear alpha beta beta alpha structure, about 145 A long. The most striking result is the demonstration of the presence of a tunnel linking the two active sites, thus permitting the diffusion of indole, the product of the alpha reaction, to the active site of the beta enzyme.
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