Complete amino acid sequence of rat liver alcohol dehydrogenase deduced from the cDNA sequence

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

Alcohol dehydrogenase (ADH) catalyzes the rate-determining reaction in the metabolism of ethanol. We report here the complete nucleotide sequence of a cDNA encoding rat liver ADH, and the deduced amino acid (aa) sequence of the protein. The rat enzyme contains a cluster of aa substitutions and an aa insertion in the region between aa residues 111 and 118, which is near the intron-exon junction reported for the human ADH gene. It also contains an additional cysteine in the highly variable region from aa residues 108-125 which may account for the unusual lability of rat ADH compared with ADH from other species.

Original languageEnglish
Pages (from-to)287-291
Number of pages5
JournalGene
Volume48
Issue number2-3
DOIs
StatePublished - 1986

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Alcohol Dehydrogenase
Amino Acid Sequence
Complementary DNA
Liver
Amino Acids
Amino Acid Substitution
Introns
Cysteine
Exons
Ethanol
Enzymes
Genes
Proteins

Keywords

  • cluster of substitutions
  • comparison to human enzyme
  • Northern blot
  • Recombinant DNA

ASJC Scopus subject areas

  • Genetics

Cite this

Complete amino acid sequence of rat liver alcohol dehydrogenase deduced from the cDNA sequence. / Crabb, David; Edenberg, Howard.

In: Gene, Vol. 48, No. 2-3, 1986, p. 287-291.

Research output: Contribution to journalArticle

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