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Characterization of Reaction Complex Structures of ATP-Utilizing Enzymes by High Resolution NMR

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NMR in Supramolecular Chemistry

Part of the book series: NATO ASI Series ((ASIC,volume 526))

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Abstract

A paradigm of biomolecular science is that the elucidation of the molecular basis of enzyme catalysis requires knowledge of the active-site structures of enzymes i.e., the precise conformational arrangement of the enzyme-bound substrates and their amino-acid environment. In this article, a review of the recent and ongoing efforts to characterize the active-site structures of a group of ATP-utilizing enzymes, by the use of high-resolution NMR methods, is presented. ATP-utilizing enzymes occur in a variety of important biochemical pathways and may be divided into three categories on the basis of the transferable moiety from ATP (see Fig. 1): 1. phosphoryl transfer (kinases), 2. nucleotidyl transfer (e.g. amino-acyl tRNA synthetases), and 3. pyrophosphoryl transfer (e.g. phosphoribosyl pyrophosphate synthetase), listed in decreasing order of their abundance in biochemical pathways. All the three categories of enzymes require a divalent cation, Mg(II) in vivo, as an obligatory component. The diversity in their catalytic roles, the obligatory cation requirement, and their ubiquity in biochemical pathways make ATP-utilizing enzymes an attractive group for structural investigations aimed at gathering insight into the molecular basis of enzyme catalysis.

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Authors and Affiliations

  1. Department of Physics, Indiana University-Purdue University at Indianapolis (IUPUI), 402 N. Blackford St., Indianapolis, IN, 46202, USA

    B. D. Nageswara Rao

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  1. B. D. Nageswara Rao
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Editors and Affiliations

  1. Departament de Química Orgànica, Universitat de Barcelona, Spain

    M. Pons

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© 1999 Springer Science+Business Media Dordrecht

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Rao, B.D.N. (1999). Characterization of Reaction Complex Structures of ATP-Utilizing Enzymes by High Resolution NMR. In: Pons, M. (eds) NMR in Supramolecular Chemistry. NATO ASI Series, vol 526. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4615-9_11

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  • DOI: https://doi.org/10.1007/978-94-011-4615-9_11

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-5950-3

  • Online ISBN: 978-94-011-4615-9

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