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Titlebook: Structural and Functional Aspects of Enzyme Catalysis; 32. Colloquium, 23. Hermann Eggerer,Robert Huber Conference proceedings 1981 Spring

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书目名称Structural and Functional Aspects of Enzyme Catalysis
副标题32. Colloquium, 23.
编辑Hermann Eggerer,Robert Huber
视频video
丛书名称Colloquium der Gesellschaft für Biologische Chemie in Mosbach Baden
图书封面Titlebook: Structural and Functional Aspects of Enzyme Catalysis; 32. Colloquium, 23.  Hermann Eggerer,Robert Huber Conference proceedings 1981 Spring
描述Enzymes perform the executive role in growth, energy conversion, and repair of a living organism. Their activity is adjusted to their en­ vironment within the cell, being turned off, switched on, or finely tuned by specific metabolites according to demands at the physiologi­ cal level. Each enzyme discovered in the long history of enzymology has revealed its own individuality. Even closely related members of a family differ in specificity, stability or regulatory properties. Despite these, at first sight overwhelming aspects of individuality, common factors of enzymic reactions have been recognized. Enzymes are stereospecific catalysts even when a nonspecific process would yield the same product. Knowledge of the detailed stereochemistry of an enzymic reaction helps to deduce reaction mechanisms and to ob­ tain insight into the specific binding of substrates at the active site. This binding close to catalytically competent groups is related to the enormous speed of enzyme-catalyzed reactions. The physical ba­ sis of rate-enhancement is understood in principle and further exploit­ ed in the design of small organic receptor molecules as model enzymes. These aspects of enzyme catalysi
出版日期Conference proceedings 1981
关键词Enzym; catalysis; enzyme; enzymes; receptor
版次1
doihttps://doi.org/10.1007/978-3-642-81738-0
isbn_softcover978-3-642-81740-3
isbn_ebook978-3-642-81738-0Series ISSN 0366-5887
issn_series 0366-5887
copyrightSpringer-Verlag Berlin Heidelberg 1981
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Design of Synthetic Molecular Receptors and Catalystsstructure, they fold up into a tertiary structure, maintained mainly by noncovalent interactions, which delineates three-dimensional crevices and cavities, whose size, shape, and binding sites are complementary to those of the substrate.
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Structural and Functional Aspects of Enzyme Catalysis978-3-642-81738-0Series ISSN 0366-5887
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