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Active Site of Ribonuclease A

  • Chapter
Artificial Nucleases

Part of the book series: Nucleic Acids and Molecular Biology ((NUCLEIC,volume 13))

Abstract

Ribonuclease A (RNase A; Ee 3.1.27.5) was perhaps the most studied enzyme of the 20th century and is the best characterized ribonuclease. The #x201C;A.#x201D; in its name refers not to its substrate specificity, but to the predominant form of the enzyme produced by the bovine pancreas. RNase A is unmodified, whereas RNase B, RNase e, and RNase D are mixtures of glycoforms. Because of its availability in large quantity and high purity, RNase A has been the object of landmark work in protein chemistry and enzymology (see Cuchillo et al. 1997; Raines 1998 and references therein). In addition, cytotoxic RNase A variants and homologues have demonstrated utility as chemotherapeutic agents (Leland and Raines 2001).

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  1. Department of Biochemistry and Department of Chemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, Wisconsin, 53706-1544, USA

    R. T. Raines

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  1. Novosibirsk Institute of Bioorganic Chemistry, 8, Lavrentiev ave., 630090, Novosibirsk, Russia

    Marina A. Zenkova

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Raines, R.T. (2004). Active Site of Ribonuclease A. In: Zenkova, M.A. (eds) Artificial Nucleases. Nucleic Acids and Molecular Biology, vol 13. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-18510-6_3

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  • DOI: https://doi.org/10.1007/978-3-642-18510-6_3

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