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The Role of Lysine-7 in Ribonuclease-A

  • Bruno Filippi
  • Gianfranco Borin
  • Fernando Marchiori
Chapter
Part of the Experimental Biology and Medicine book series (EBAM, volume 19)

Abstract

Bovine pancreatic ribonuclease A(RNase A) catalyzes the hydrolysis of RNA by a two-stage mechanism. The first step is a transphosphorylation to give an oligonucleotide terminating in a pyrimidine 2′-3′-cyclic phosphate. The second is the hydrolysis of the cyclic phosphate to give a terminal 3′-phosphate. At present it is not clear whether the invariant lysine-7 plays any part in the enzyme activity. Chemical modifications of the ε-ammonium group give derivatives with 15–30% activity, but substrate binding has been observed to be unaffected. On the other hand, the X-ray crystallography data, while confirming that Lys-7 is located relatively close to and with free access to the active site, strongly suggest that this residue is still too far away from the site to interact with the substrate (1).

Keywords

Circular Dichroism Ammonium Group Cyclic Phosphate Electronic Structure Theory Total Ionic Strength 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Richards, F.M. and Wyckoff, H.W. (1971) The Enzymes, 3rd Ed., 4, 647–806.CrossRefGoogle Scholar
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    Komoriya, A. and Chalken, I.M. (1982), J. Biol. Chem. 257, 2599–2604.PubMedGoogle Scholar
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    Grourke, M.T. and Gibbs, J.H. (1971) Biopolymers 10, 795–808.PubMedCrossRefGoogle Scholar
  4. 4.
    Marchiori, F., Borin, G. and Moroder, L. (1974) Int. J. Pep. Prot. Res. 6, 419–434.CrossRefGoogle Scholar
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    Deakyne, C.A. and Allen, L.C. (1979) J. Am. Chem. Soc. 101, 3951–3959.CrossRefGoogle Scholar

Copyright information

© The Humana Press Inc. 1987

Authors and Affiliations

  • Bruno Filippi
    • 1
  • Gianfranco Borin
    • 1
  • Fernando Marchiori
    • 1
  1. 1.Department of Organic Chemistry, Biopolymer Research CenterUniversity of PaduaPaduaItaly

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