The discovery of a new family of mammalian enzymes for repair of oxidatively damaged DNA, and its physiological implications

Tapas Hazra, Tadahide Izumi, Y. Wah Kow, Sankar Mitra

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

Oxidatively damaged bases in the genome are likely to be responsible for mutations leading to sporadic carcinogenesis. Two structurally similar DNA glycosylases, NTH1 and OGG1, which are able to excise most of these damaged bases, were identified previously in mammalian cells. A distinct family, consisting of two human DNA glycosylases orthologous to enzymes in Escherichia coli, has recently been characterized; they have overlapping substrate ranges with NTH1 and OGG1. The presence of multiple enzymes with potential back-up functions underscores the importance of removing both endogenously and exogenously generated oxidatively damaged bases from the genome, and may explain why no cancer or other disease phenotype has so far been linked to the deficiency of a single DNA glycosylase.

Original languageEnglish (US)
Pages (from-to)155-157
Number of pages3
JournalCarcinogenesis
Volume24
Issue number2
DOIs
StatePublished - Feb 1 2003

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DNA Glycosylases
DNA
Enzymes
Genome
Carcinogenesis
Escherichia coli
Phenotype
Mutation
Neoplasms

ASJC Scopus subject areas

  • Cancer Research

Cite this

The discovery of a new family of mammalian enzymes for repair of oxidatively damaged DNA, and its physiological implications. / Hazra, Tapas; Izumi, Tadahide; Kow, Y. Wah; Mitra, Sankar.

In: Carcinogenesis, Vol. 24, No. 2, 01.02.2003, p. 155-157.

Research output: Contribution to journalArticle

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