Ribonucleases A and T1 Comparable Mechanisms of RNA Cleavage with Different Active Site Geometries

  • W. Saenger
  • R. Arni
  • M. Maslowska
  • A. Pähler
  • U. Heinemann
Part of the NATO ASI Series book series (NSSA, volume 126)


There are a variety of enzymes which cleave the phosphodiester link in ribo- and deoxyribonucleic acids. They exhibit different catalytic activities, different mechanisms of cleavage, and different three-dimensional structures. The best known examples are DNase I which acts upon single and double stranded DNA , staphylococcal nuclease which cleaves P-0 bonds in RNA and DNA single strands2 , and the two RNases A and T1 which cut at the 3′-end of pyrimidine and guanosine nucleotides respectively3-5 . Although the two RNases have different molecular topology, the mechanism of hydrolysis is similar and suggestive of a comparable active site geometry. Since high resolution crystal structures are available (1.5Å for RNase A and 2.oÅ for RNase T1)3-5, a study of the arrangement of the functional amino acids in the1 active sites of the two enzymes is of interest.


Active Site Residue Pancreatic Ribonuclease Staphylococcal Nuclease Functional Amino Acid Guanosine Nucleotide 


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Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • W. Saenger
    • 1
  • R. Arni
    • 1
  • M. Maslowska
    • 1
  • A. Pähler
    • 1
  • U. Heinemann
    • 1
  1. 1.Institut für KristallographieFreie Universität BerlinBerlin 33Germany

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