Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources

J Biol Chem. 1989 Sep 25;264(27):15818-23.


Rat liver serine dehydratase cDNA was used to screen a human liver cDNA library in lambda gt11. One positive clone occurred in every 5,000 clones. Fifteen positive clones were plaque purified. The largest cDNA obtained contained an open reading frame of 987 base pairs, and 5' and 3' noncoding regions of 89 and 317 base pairs, respectively. The deduced amino acid sequence, with a calculated Mr of 34,615, was similar to that of rat liver serine dehydratase except for the absence of a segment consisting of 36 amino acid residues. In vitro transcription/translation with the cDNA resulted in the formation of a polypeptide with an Mr of approximately 35,000, which cross-reacted with the anti-rat serine dehydratase antibody. These results suggest that the human serine dehydratase is structurally cognate with the rat enzyme. Moreover, portions of the sequence postulated to be essential for activity in microbial threonine dehydratases are found in the mammalian serine dehydratases, suggesting that hydroxyamino and dehydratases may have originated from a common ancestor.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular*
  • DNA / genetics*
  • Escherichia coli / enzymology
  • Genes
  • Humans
  • L-Serine Dehydratase / genetics*
  • Liver / enzymology*
  • Molecular Sequence Data
  • Protein Conformation
  • Rats
  • Restriction Mapping
  • Saccharomyces cerevisiae / enzymology
  • Sequence Homology, Nucleic Acid
  • Threonine Dehydratase / genetics*


  • DNA
  • L-Serine Dehydratase
  • Threonine Dehydratase

Associated data

  • GENBANK/J05037