Potent Inhibition of  Hha I DNA Methylase by the Aglycon of 2‐(1 H )‐Pyrimidinone Riboside (Zebularine) at the G C GC Recognition Domain | Zendy

MARQUEZ VICTOR E. | Zendy; ERITJA RAMON | Zendy; KELLEY JAMES A. | Zendy; VANBEMMEL DANA | Zendy; CHRISTMAN JUDITH K. | Zendy

Premium

Potent Inhibition of Hha I DNA Methylase by the Aglycon of 2‐(1 H )‐Pyrimidinone Riboside (Zebularine) at the G C GC Recognition Domain

Author(s) -

MARQUEZ VICTOR E.,

ERITJA RAMON,

KELLEY JAMES A.,

VANBEMMEL DANA,

CHRISTMAN JUDITH K.

Publication year - 2003

Publication title -

annals of the new york academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.712

H-Index - 248

eISSN - 1749-6632

pISSN - 0077-8923

DOI - 10.1196/annals.1281.014

Subject(s) - chemistry , riboside , dna methyltransferase , dna , methyltransferase , biochemistry , stereochemistry , biophysics , methylation , biology

A bstract : A short oligodeoxynucleotide (ODN) with 2‐(1H)‐pyrimidinone at the Hha I DNA methyltransferase target site (GCGC) is shown to induce a level of inhibition of methyl transfer and thermal stability of the complex with the enzyme identical to that achieved with a similar ODN substituted with 5‐azacytosine. The drugs responsible for these effects—zebularine and 5‐azacytidine/2′‐deoxy‐5‐azacytidine—are contrasted in terms of chemical stability and possible metabolic activation by a brief structure‐activity analysis.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research