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Interaction of Adenosine with Adenosine-Binding Protein, S-Adenosylhomocysteine Hydrolase

  • Chapter
Regulatory Function of Adenosine

Part of the book series: Developments in Pharmacology ((DIPH,volume 2))

Abstract

Soluble adenosine-binding proteins were first described by Yuh and Tao in rabbit erythrocytes [1], and similar proteins were later isolated from various eukaryotes [2–8]. The physiological role of these binding proteins for adenosine (Ado) remained obscure until Hershfield [9] and Hershfield and Kredich [10] demonstrated that such proteins from human placenta, spleen, and lymphoblasts were identical to S-adenosylhomocysteine (AdoHcy) hydrolase (EC: 3.3.1.1), the enzyme responsible for the metabolic degradation of the endogenous transmethylase inhibitor, AdoHcy [11]. This finding has been confirmed by others [12–14]. This chapter is a brief review of the properties of AdoHcy hydrolase, with emphasis on the interaction of the enzyme with Ado.

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Authors
  1. Per Magne Ueland
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Editors and Affiliations

  1. Department of Physiology, University of Virginia School of Medicine, Charlottesville, Virginia, USA

    Robert M. Berne  & Rafael Rubio  & 

  2. Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia, USA

    Theodore W. Rall

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© 1983 Martinus Nijhoff Publishers, The Hague

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Ueland, P.M. (1983). Interaction of Adenosine with Adenosine-Binding Protein, S-Adenosylhomocysteine Hydrolase. In: Berne, R.M., Rall, T.W., Rubio, R. (eds) Regulatory Function of Adenosine. Developments in Pharmacology, vol 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3909-0_10

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  • DOI: https://doi.org/10.1007/978-1-4613-3909-0_10

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-3911-3

  • Online ISBN: 978-1-4613-3909-0

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