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Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3' endonuclease, from Escherichia coli.
TLDR
A novel endonuclease from Escherichia coli that recognizes deoxyinosine, a deamination product of deoxyadenosine in DNA, which is different from the known hypoxanthine DNA N-glycosylases which have been partially characterized in E. coli.
Cleavage of Insertion/Deletion Mismatches, Flap and Pseudo-Y DNA Structures by Deoxyinosine 3′-Endonuclease from Escherichia coli*
  • M. Yao, Y. Kow
  • Biology, Chemistry
    The Journal of Biological Chemistry
  • 29 November 1996
Deoxyinosine 3′-endonuclease, an Escherichia coli repair enzyme that recognizes and cleaves DNA containing deoxyinosine and base mismatches, can cleave heteroduplexes containing a hairpin or unpaired
Further characterization of Escherichia coli endonuclease V. Mechanism of recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA.
  • M. Yao, Y. Kow
  • Biology, Chemistry
    The Journal of biological chemistry
  • 5 December 1997
TLDR
Using enzyme purified from an overproducing strain, the deoxyinosine- and mismatch-specific activities of endonuclease V was found to have different divalent metal requirements and a model for the mechanism of substrate recognition is proposed to explain these different activities.
Complex structure of the DNA-binding domain of AdpA, the global transcription factor in Streptomyces griseus, and a target duplex DNA reveals the structural basis of its tolerant DNA sequence
TLDR
AdpA-DBD confers tolerant DNA sequence specificity to AdpA, allowing it to control hundreds of genes as a global transcription factor, and reveals its unique manner of DNA recognition.
Interaction of Deoxyinosine 3′-Endonuclease from Escherichia coli with DNA Containing Deoxyinosine (*)
  • M. Yao, Y. Kow
  • Biology, Chemistry
    The Journal of Biological Chemistry
  • 1 December 1995
TLDR
Deoxyinosine 3′-endonuclease exhibited similar affinities for both the substrate and the nicked duplex product and thus remained bound to the DNA after the cleavage reaction, and a model is proposed for the interaction of deoxyinosinesine 3″-endonUClease with DNA containing de Oxyinosine.
Strand-specific cleavage of mismatch-containing DNA by deoxyinosine 3'-endonuclease from Escherichia coli.
  • M. Yao, Y. Kow
  • Biology, Chemistry
    The Journal of biological chemistry
  • 16 December 1994
TLDR
Interestingly, deoxyinosine 3'endonuclease showed strong strand specificity on DNA containing mismatches, and only one strand of the mismatch-containing DNA was nicked by the enzyme, and this strand specificity of mismatch cleavage was not affected by the nature of the mismatches.
Deoxyinosine 3′ Endonuclease, a Novel Deoxyinosine‐Specific Endonuclease from Escherichia coli
TLDR
The enzyme is different from hypoxanthine DNA glycosylase and displays a novel AF' endonuclease activity different from those of class I and class I1 AP endonucleases, which was found to be active on oligonucleotides containing I/T, I/C, I-A, and I/G pairs.
Further Characterization of Escherichia coliEndonuclease V
  • M. Yao, Y. Kow
  • Biology, Chemistry
    The Journal of Biological Chemistry
  • 5 December 1997
TLDR
Using enzyme purified from an overproducing strain, the deoxyinosine- and mismatch-specific activities of endonuclease V was found to have different divalent metal requirements and a model for the mechanism of substrate recognition is proposed to explain these different activities.
Genomic structure of the rat major AP endonuclease gene (Apex) with an adjacent putative O-sialoglycoprotease gene (Prsmg1/Gcpl1) and a processed Apex pseudogene (Apexp1).
TLDR
Calculation of nucleotide substitution rates suggests that the immediate, active progenitor of Apexp1 arose 23 millions years ago and that the non-functionalization occurred 15 million years ago.
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