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標題: Titlebook: Allosteric Regulatory Enzymes; Thomas Traut Book 2008 Springer-Verlag US 2008 Aspartat.DNA.Glycogen.Nucleotide.RNA.enzymes.metabolism.tran [打印本頁]

作者: Cataplexy    時間: 2025-3-21 16:28
書目名稱Allosteric Regulatory Enzymes影響因子(影響力)




書目名稱Allosteric Regulatory Enzymes影響因子(影響力)學科排名




書目名稱Allosteric Regulatory Enzymes網(wǎng)絡公開度




書目名稱Allosteric Regulatory Enzymes網(wǎng)絡公開度學科排名




書目名稱Allosteric Regulatory Enzymes被引頻次




書目名稱Allosteric Regulatory Enzymes被引頻次學科排名




書目名稱Allosteric Regulatory Enzymes年度引用




書目名稱Allosteric Regulatory Enzymes年度引用學科排名




書目名稱Allosteric Regulatory Enzymes讀者反饋




書目名稱Allosteric Regulatory Enzymes讀者反饋學科排名





作者: coalition    時間: 2025-3-21 23:47
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
作者: 公共汽車    時間: 2025-3-22 04:24
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
作者: Systemic    時間: 2025-3-23 02:31
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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作者: 黃油沒有    時間: 2025-3-23 12:56
Introduction To V-Type Enzymesa comparable change in their affinity for the substrate. When such enzymes are in a normal metabolic pathway, changes in the maximum activity can be up to 30-fold. To be included in this category, enzymes must have at least a doubling in .max, so that this allosteric effect can be physiologically or
作者: 煩擾    時間: 2025-3-23 14:33
G Proteinstivate various cellular receptors and protein kinases. A GTPase activating protein (GAP) can increase this hydrolytic step by up to five orders of magnitude. For this feature these enzymes are called .-type enzymes, even though many G proteins also have significant changes in .d for the bound substr
作者: PUT    時間: 2025-3-23 18:28
Protein Kinases themselves regulated by phosphorylation, as well as by separate regulatory ligands. The effects of phosphorylation and ligand binding may also be synergistic. Many of these protein kinase activation signals are propagated in sequential protein phosphorylation steps, and the total activation can be
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isms 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..978-1-4419-4453-5978-0-387-72891-9
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http://image.papertrans.cn/a/image/153839.jpg
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Classical Vertical References of Albania,ake the needed product almost immediately available. Almost all enzymes are proteins that fold into domains. The majority of enzymes contains one domain (simple enzymes), while many are composed of two or more domains (allosteric enzymes and multifunctional proteins). Most enzymes are designed to fu
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https://doi.org/10.1007/978-3-658-32594-7h employ a change in affinity for the substrate to alter activity. One of the groups experiences only a change in affinity for the principal substrate, while keeping the maximum rate fairly constant (. enzymes). The second group also demonstrates significant changes in affinity for the main substrat
作者: Heresy    時間: 2025-3-25 22:36
GUI for PSBN-based decision verificationfor 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
作者: 間接    時間: 2025-3-26 02:54
GUI for PSBN-based decision verificationefold difference in the normal oxygen concentration between the lungs and the tissues, cooperativity in the affinity for oxygen is necessary to achieve efficient delivery of oxygen. This cooperativity results mainly from a conformational change in the quaternary structure of the hemoglobin tetramer,
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Development of Consumer Finance in East Asiain 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
作者: 思考而得    時間: 2025-3-26 16:53

作者: 燒烤    時間: 2025-3-26 23:15
Progress in Automatic Production of Braillea comparable change in their affinity for the substrate. When such enzymes are in a normal metabolic pathway, changes in the maximum activity can be up to 30-fold. To be included in this category, enzymes must have at least a doubling in .max, so that this allosteric effect can be physiologically or
作者: 1分開    時間: 2025-3-27 04:04
A. Da Ronch,R. Spinabelli,A. Braggiottitivate various cellular receptors and protein kinases. A GTPase activating protein (GAP) can increase this hydrolytic step by up to five orders of magnitude. For this feature these enzymes are called .-type enzymes, even though many G proteins also have significant changes in .d for the bound substr
作者: Demulcent    時間: 2025-3-27 08:15
J. Conter,S. Alet,P. Puech,A. Bruel themselves regulated by phosphorylation, as well as by separate regulatory ligands. The effects of phosphorylation and ligand binding may also be synergistic. Many of these protein kinase activation signals are propagated in sequential protein phosphorylation steps, and the total activation can be
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https://doi.org/10.1007/978-3-658-32594-7, while keeping the maximum rate fairly constant (. enzymes). The second group also demonstrates significant changes in affinity for the main substrate, and in addition has large changes in the maximum rate (. enzymes). The greatest changes in .max are for enzymes that act as regulatory switches.
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作者: 用肘    時間: 2025-3-29 02:16
Phosphofructokinasephoenolpyruvate and activated by AMP. The larger enzyme uses ATP, and has additional regulatory sites. A special site for fructose-2,6-bisphosphate has resulted in this activator being obligatory for many versions of the enzyme. The larger enzyme is also activated by ADP/AMP, and inhibited by ATP, and citrate.
作者: 隱語    時間: 2025-3-29 05:06
Introduction To V-Type Enzymesp to 30-fold. To be included in this category, enzymes must have at least a doubling in .max, so that this allosteric effect can be physiologically or experimentally meaningful. When these enzyme activities are part of a regulatory switch, the change in activity may exceed 100,000-fold.
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作者: 榮幸    時間: 2025-3-29 14:33
https://doi.org/10.1007/978-3-658-32594-7to make the binding range narrower, so that saturation is approached below [L] = 10.d, by changing the affinity for the ligand. The effect of negative cooperativity is to extend the binding range so that saturation is never approached under physiological concentrations of the ligand.
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作者: FACT    時間: 2025-3-29 19:54
Development of Consumer Finance in East Asiaof the microbial enzymes have one regulatory site, while the enzyme from . and most eukaryotes normally has two. Regulation at these sites by nucleotide effectors permits the enzyme to alter its selection for any of the four ribonucleotide substrates.
作者: 改革運動    時間: 2025-3-30 03:38
A. Da Ronch,R. Spinabelli,A. Braggiottiate or allosteric effector. GAP is an inhibitor, since by activating the GTPase rate it limits the time for the protein to be active. Guanine nucleotide exchange factors (GEFs) lower the affinity for the tightly bound GDP and promote replacement by GTP.
作者: 問到了燒瓶    時間: 2025-3-30 06:44





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