Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

A DNA enzyme with N-glycosylase activity

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Sheppard, T. L.
  • Ordoukhanian, Phillip
  • Joyce, Gerald

publication date

  • July 2000

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • In vitro evolution was used to develop a DNA enzyme that catalyzes the site-specific depurination of DNA with a catalytic rate enhancement of about 10(6)-fold. The reaction involves hydrolysis of the N-glycosidic bond of a particular deoxyguanosine residue, leading to DNA strand scission at the apurinic site. The DNA enzyme contains 93 nucleotides and is structurally complex. It has an absolute requirement for a divalent metal cation and exhibits optimal activity at about pH 5. The mechanism of the reaction was confirmed by analysis of the cleavage products by using HPLC and mass spectrometry. The isolation and characterization of an N-glycosylase DNA enzyme demonstrates that single-stranded DNA, like RNA and proteins, can form a complex tertiary structure and catalyze a difficult biochemical transformation. This DNA enzyme provides a new approach for the site-specific cleavage of DNA molecules.

subject areas

  • Catalysis
  • DNA
  • DNA Glycosylases
  • DNA Repair
  • Deoxyguanosine
  • Directed Molecular Evolution
  • Models, Chemical
  • N-Glycosyl Hydrolases
  • Nucleic Acid Conformation
  • Oligodeoxyribonucleotides
  • Selection, Genetic
scroll to property group menus

Research

keywords

  • DNA cleavage
  • DNA repair
  • depurination
  • in vitro evolution
  • nucleic acid catalysis
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.97.14.7802

PubMed ID

  • 10884411
scroll to property group menus

Additional Document Info

start page

  • 7802

end page

  • 7807

volume

  • 97

issue

  • 14

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support