Abstract
In order to clarify the cause of hereditary orotic aciduria, UMP synthase (a multifunctional protein having both orotate phosphoribosyltransferase and OMP decarboxylase activities) was purified from normal human erythrocytes. The enzyme protein had a molecular weight of 51,000. Then a cDNA fragment of mouse OMP decarboxylase was isolated from a λgtll mouse spleen cDNA library by the use of a synthesized oligonucleotide probe. Screening of a λgtll human placenta cDNA library yielded positive clones which hybridized strongly to the mouse cDNA fragment. Analysis of the nucleotide sequence of the entire cDNA insert (1.7 kb) of one of the clones indicated that it contained an open reading frame (1,473 bp) encoding a protein with a molecular weight of 53,496. The deduced amino acid sequence of the 3′-half of the insert showed 89% homology with that deduced from Ehrlich ascites carcinoma OMP decarboxylase cDNA. Northern blot analysis revealed a presence of a single band of approximately 1.8 kb, which suggests that the cloned cDNA contains the whole message for human UMP synthase.
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Suchi, M., Harada, N., Tsuboi, T. et al. 152 MOLECULAR CLONING OF HUMAN UMP SYNTHASE. Pediatr Res 24, 136 (1988). https://doi.org/10.1203/00006450-198807000-00176
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DOI: https://doi.org/10.1203/00006450-198807000-00176