CMP-N-Acetylneuraminic acid hydroxylase is exclusively inactive in humans

Biochem Biophys Res Commun. 1998 Jul 20;248(2):330-3. doi: 10.1006/bbrc.1998.8946.


We cloned cDNAs for mouse and human CMP-N-acetylneuraminic acid (CMP-NeuAc) hydroxylases and showed that the human CMP-NeuAc hydroxylase protein is inactive because of a partial deletion in the hydroxylase gene. We report here that no other active CMP-NeuAc hydroxylases are present in humans. Southern blot analysis showed that the human homologue of the mouse CMP-NeuAc hydroxylase is one gene in the human genome and no other homologues of the mouse hydroxylase exist in human genome. The mouse and the human CMP-NeuAc hydroxylases were mapped to chromosome 13A3 and chromosome 6p22, respectively, by fluorescence in situ hybridization. The chromosomal location of the human hydroxylase is syntenic to that of the mouse hydroxylase. These results demonstrate that the human CMP-NeuAc hydroxylase is the only homologue of the mouse hydroxylase, and CMP-NeuAc hydroxylase is exclusively inactive in humans.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Southern
  • Chromosome Mapping
  • Chromosomes, Human, Pair 6 / genetics*
  • Cloning, Molecular
  • Gene Deletion
  • Humans
  • In Situ Hybridization, Fluorescence
  • Mice
  • Mixed Function Oxygenases / genetics*
  • Mixed Function Oxygenases / metabolism
  • N-Acetylneuraminic Acid / metabolism
  • Neuraminic Acids / metabolism


  • Neuraminic Acids
  • N-glycolylneuraminic acid
  • Mixed Function Oxygenases
  • CMPacetylneuraminate monooxygenase
  • N-Acetylneuraminic Acid