Isolation and characterization of the gene coding for human cytidine deaminase

Silvia Demontis, Mineko Terao, Massimo Brivio, Stefania Zanotta, Maurizio Bruschi, Enrico Garattini

Research output: Contribution to journalArticle


The human gene coding for cytidine deaminase (CD), the enzyme which catalyzes the deamination of cytidine and deoxycytidine to uridine and deoxyuridine, was isolated and structurally characterized. CD is a single copy gene with a length of 31 kb and consists of four exons. Exon-intron junctions do not bracket functional domains of the encoded protein as the boundary between exons 2 and 3 interrupts the catalytically important zinc- finger domain, which is well conserved along phylogenesis. 5'-RACE and RNase mapping experiments identify one major and multiple other minor transcription initiation sites, which are present in placenta as well as in the myeloid cell lines, HL-60 and U937. The 5'-flanking region of the gene contains an orientation-dependent functional promoter and is characterized by the presence of several potential sites for the binding of known transcriptional factors.

Original languageEnglish
Pages (from-to)323-333
Number of pages11
JournalBBA - Gene Structure and Expression
Issue number3
Publication statusPublished - Dec 22 1998


  • 1-̄-D- Arabinofuranosylcytosine
  • Cytidine
  • Cytidine deaminase
  • Gene
  • Leukemia
  • Structure

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Structural Biology
  • Biophysics

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