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Titlebook: Allosteric Regulatory Enzymes; Thomas Traut Book 2008 Springer-Verlag US 2008 Aspartat.DNA.Glycogen.Nucleotide.RNA.enzymes.metabolism.tran

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發(fā)表于 2025-3-21 16:28:04 | 只看該作者 |倒序瀏覽 |閱讀模式
期刊全稱Allosteric Regulatory Enzymes
影響因子2023Thomas Traut
視頻videohttp://file.papertrans.cn/154/153839/153839.mp4
發(fā)行地址Covers the most recent developments in the analysis of allosteric enzymes.Extensively illustrated to clarify kinetic and regulatory properties.Discusses recently created crystal structures of the enzy
圖書封面Titlebook: Allosteric Regulatory Enzymes;  Thomas Traut Book 2008 Springer-Verlag US 2008 Aspartat.DNA.Glycogen.Nucleotide.RNA.enzymes.metabolism.tran
影響因子.All enzymes are remarkable since they have the ability to increase the rate of a chemical reaction, often by more than a billion-fold. Allosteric enzymes are even more amazing because the have the additional ability to change their rate in response to cellular activators or inhibitors. This enables them to control the pathway in which they are the regulatory enzyme. Since the effector molecules represent the current status of the cell for a given metabolic pathway, this results in very responsive and balanced metabolic states, and makes it possible for cells and organisms to be appropriately dynamic, and responsive, in a changing environment. This book provides a logical introduction to the limits for enzyme function as dictated by the factors that are limits for life. This book presents a complete description of all the mechanisms used for changing enzyme acticity. Eight enzymes are used as model systems after extensive study of their mechanisms. Wherever possible, the human form of the enzyme is used to illustrate the regulatory features..
Pindex Book 2008
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發(fā)表于 2025-3-21 23:47:09 | 只看該作者
The Limits For Life Define The Limits For EnzymesFor metabolic enzymes .cat’s must be ≥1 s–1, and are generally 10–3,000 s–1. It then follows that for metabolic enzymes . values are generally limited to be between 1 μM and 1 mM. While increased . values would enable much faster .cat’s, there is a clear need for enzymes to be sufficiently discrimin
板凳
發(fā)表于 2025-3-22 04:24:20 | 只看該作者
Enzyme Kinetics–Burk, Eadie– Hofstee, and Hill. The . binding range for a ligand with constant affinity is nearly 100-fold. At [L] ≤ 0.1.d, binding becomes ineffective. At [L] ≥ 10.d, binding approaches saturation. This effective binding range is easily remembered as the .. The effect of positive cooperativity is
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Kinetics Of Allosteric Enzymesfor the different subunits. Most .-type enzymes have positive cooperativity; a limited number of regulatory enzymes have negative cooperativity. This controlled change in affinity makes the enzyme more sensitive to changes in substrate concentration (positive cooperativity), or dampens the enzyme’s
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Phosphofructokinasee smaller enzyme in microbes has versions that may use ATP, ADP, or pyrophosphate as the phosphate donor. These enzymes are normally inhibited by phosphoenolpyruvate and activated by AMP. The larger enzyme uses ATP, and has additional regulatory sites. A special site for fructose-2,6-bisphosphate ha
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Ribonucleotide Reductasein a reducing environment, additional forms evolved to function in an aerobic state. While the different classes of this enzyme have different cofactors, and different mechanisms for generating the free radical necessary for the reaction, they have retained many of the key regulatory features. Most
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