Published October 1994 | Version v1
Report Open

Catalytic activity of nuclease P1: Experiment and theory

  • 1. Pacific Northwest Lab., Richland, WA (United States)
  • 2. Roswell Park Cancer Institute, Buffalo, New York (United States)

Description

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. Nuclease Pl 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 Pl 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 Pl. 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

Availability note (English)

MF available from INIS under the Report Number; Also available from OSTI as DE95004956; NTIS; US Govt. Printing Office Dep.

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Additional details

Publishing Information

Imprint Pagination
9 p.
Report number
PNL-SA--25462

Conference

Title
relationships at early times.
Acronym
International workshop on radiation damage in DNA
Dates
1-6 Oct 1994.
Place
Gleneden, OR (United States).

Optional Information

Contract/Grant/Project number
Contract AC06-76RL01830
Funding organization
USDOE, Washington, DC (United States).
Secondary number(s)
CONF-9410280--1.