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• W2582382866 abstract "This chapter discusses the applications of kinetic methods to aminoacyl-tRNA synthetases. It discusses steady state-initial velocity kinetics that are a useful tool in the study of enzyme mechanisms. Although they cannot be used to prove a particular mechanism, they can often exclude certain possibilities. This model necessarily involves a sequential mechanism, in which all substrates add to the enzyme before a product is released. The chapter presents the method for measuring the AMP-dependent-tRNA↔AA tRNA exchange. This reaction, when carried out in the absence of ATP, PPI, and amino acid, provides a means for measuring E:AA-AMP formation from the product side. The chapter discusses conventional kinetic analyses that are complicated by the necessity of measuring complex functions. Several approaches have been developed for measuring binding constants and velocity constants independently. Binding of substrates and other ligands to aminoacyl-tRNA synthetases has been studied by three methods: protection against thermal denaturation, modification of fluorescence of the enzyme, and equilibrium dialysis. Velocity constants of partial reactions have been studied also by three methods: rapid binding of enzyme to nitrocellulose filters, transfer of amino acid from the enzyme-aminoacyl adenylate complex and stopped-flow measurements with a fluorescence reporter group." @default.
• W2582382866 created "2017-02-03" @default.
• W2582382866 creator A5049254514 @default.
• W2582382866 creator A5067629632 @default.
• W2582382866 date "1974-01-01" @default.
• W2582382866 modified "2023-09-27" @default.
• W2582382866 title "[50] Applications of kinetic methods to aminoacyl-tRNA synthetases" @default.
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• W2582382866 doi "https://doi.org/10.1016/0076-6879(74)29055-4" @default.
• W2582382866 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4368426" @default.
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