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 journalArticlepeer-review


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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