Molecular cloning of mouse alcohol dehydrogenase-b2 cDNA: Nucleotide sequences of the class III ADH genes evolve slowly even for silent substitutions

Man Wook Hur, Wei Hsien Ho, Celeste J. Brown, David Goldman, Howard J. Edenberg

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16 Scopus citations


We have cloned and sequenced a cDNA encoding the mouse class III alcohol dehydrogenase, Adh-B2. Adh-B2 mRNA is detectable in all the mouse tissues tested. Class III ADHs are highly conserved: the deduced ammo acid sequence of the mouse Adh-B2 is 91 to 97% identical to the human, horse and rat liver enzymes. The mouse Adh-B2 cDNA is 87% identical in nucleotide sequence to the human χADH cDNA. Previously, a slower rate of evolutionary divergence of the amino acid sequences of class III ADH proteins was detected and ascribed to functional constraints upon the protein. Our analysis of the nucleotide sequences demonstrates that this cannot be the entire explanation, since the rate of silent (synonymous) nucleotide substitutions is also lower in the class III ADHs than in the class I ADHs.

Original languageEnglish (US)
Pages (from-to)167-175
Number of pages9
JournalMitochondrial DNA
Issue number3
StatePublished - Jan 1 1992



  • Alcohol dehydrogenase
  • CDNA
  • Evolution
  • Formaldehyde dehydrogenase
  • Silent substitutions

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Biochemistry
  • Endocrinology

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