Catalytic activity of nuclease P1: Experiment and theory Page: 3 of 10
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CATALYTIC ACTIVITY OF NUCLEASE P1: EXPERIMENT AND THEORY
J. M. Falcone, M. Shibata and H. C. Box
Roswell Park Cancer Institute
Buffalo, NY 14263
J. H. Miller
Pacific Northwest Laboratory
Richland WA 99352
Nuclease P1 from Penicillium citrinum is a zinc dependent glyco-enzyme
that recognizes single stranded DNA and RNA as substrates and hydrolyzes the
phosphate ester bond. As a single chain of 270 amino acid residues, the enzyme has
a molecular mass of about 36 kilodaltons (Maekawa et al. 1991). Although it exhibits
3'-phosphatase activity, P1 is primarily an endonuclease that is capable of
hydrolyzing single stranded DNA completely to the level of mononucleosides.
Nuclease P1 seems to recognize particular conformations of the phosphodiester
backbone and shows significant variation in the rate of hydrolytic activity
depending upon which nucleosides are coupled by the phosphodiester bond. The
efficiency of nuclease P1 in hydrolyzing the phosphodiester bonds of a substrate can
be altered by modifications to one of the substrate bases induced by ionizing
radiation or oxidative stress. Measurements have been made of the effect of several
radiation induced lesions on the catalytic rate of nuclease P1. A model of the
structure of the enzyme has been constructed in order to better understand the
binding and activity of this enzyme on various ssDNA substrates.
Biochemical Materials and Methods
Normal dinucleoside monophosphates were purchased from Sigma and
nuclease P1 was purchased from Boehringer Mannheim. Modified dinucleoside
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Miller, J.H.; Falcone, J.M.; Shibata, M. & Box, H.C. Catalytic activity of nuclease P1: Experiment and theory, article, October 1, 1994; Richland, Washington. (digital.library.unt.edu/ark:/67531/metadc666014/m1/3/: accessed February 23, 2019), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.