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

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Abstract

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.

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Journal

Journal ID (iso-abbrev): Biochem Biophys Res Commun

Title: Biochemical and biophysical research communications

Publisher: Elsevier BV

ISSN: 0006-291X

ISSN (Print): 0006-291X

Publication date (Electronic): Jul 20 1998

Volume: 248

Issue: 2

Affiliations

[1 ] Department of Membrane Biochemistry, Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, 113-8613, Japan.

Article

Publisher Item ID: S0006-291X(98)98946-X

DOI: 10.1006/bbrc.1998.8946

PubMed ID: 9675135

SO-VID: 9a149a87-1fc9-4dac-9888-adf3f71834d8

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