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Titlebook: Enzyme Dynamics and Regulation; P. Boon Chock,Charles Y. Huang,Jerry H. Wang Book 1988 Springer-Verlag New York Inc. 1988 ATP.Aspartat.Chl

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Mechanism of Activation of Calmodulin-Dependent Phosphatase by Divalent Metal Ionsme can be readily appreciated from its participation in regulations involving Ca.—CaM and phosphorylation/dephosphorylation, its abundance and ubiquity in various tissues, and its action on diverse substrates (see ref. 1 for review), which include phosphatase inhibitor I, the regulatory subunit of c
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Studies on the Mechanism and Molecular Mode of Regulation of Fructose-1,6-bisphosphatasesphatase (FBPase) (EC 3.1.3.11). FBPase and phosphofructokinase constitute a highly regulated system for the futile cycle of FBP synthesis and degradation, a focal point in the antagonistic control of glycolysis and gluconeogenesis in the liver. The hydrolysis of FBP by FBPase is inhibited by AMP an
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Conformational Dynamics in RNA—Protein Interactions: Immobilization of the Functional Domains in tRNcritical roles in the recognition processes. Conformational flexibility in proteins and its functional significance in some proteins have been elucidated (1). Relatively little is known about the segmental movement in RNA. Specific interactions of tRNA and cognate synthetases have provided model sys
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Cu,Zn Superoxide Dismutase: A Case of Metalloenzyme Catalysis in Which the Protein Moiety Plays a Mas enzyme consists of two identical subunits of 16 kD, each containing a cataly­tically active copper ion and a zinc ion, which shares a common ligand—the imidazole of His 61—with the copper. It has been demonstrated (3, 4) that the enzyme-catalyzed superoxide ion dismutation proceeds by a cyclic oxi
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Dynamic Participation of Protein Domains in Catalysis by 2-Oxo Acid Dehydrogenase Multienzyme Compleve steps in the oxidative decarboxylation of the relevant 2-oxo acids, notably pyruvate, 2-oxoglutarate, and branched-chain 2-oxo acids derived from transamination of isoleucine, leucine, and valine. The overall reaction scheme is shown in Fig. 12.1.
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