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Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase
J E Flach1, J K Reichardt, L J Elsas
1Department of Pediatrics, Emory University, Atlanta, GA 30322.
Molecular Biology & Medicine
|August 1, 1990
Summary
A revised human galactose-1-phosphate uridyl transferase (GALT) cDNA sequence was determined. This updated sequence reveals greater amino acid similarity between human, E. coli, and yeast GALT enzymes.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- The enzyme galactose-1-phosphate uridyl transferase (GALT) is crucial for carbohydrate metabolism.
- Previous studies provided an initial sequence for human GALT cDNA, but revisions may enhance understanding.
Purpose of the Study:
- To report a revised sequence of the human galactose-1-phosphate uridyl transferase (GALT) cDNA.
- To analyze the encoded protein and compare its conservation with homologous enzymes.
Main Methods:
- Isolation of a cDNA clone from a transformed human lymphoblast cell line.
- Amplification of the cDNA sequence using polymerase chain reaction (PCR).
- Sequence analysis and comparison with homologous enzymes from other species.
Main Results:
- A revised cDNA sequence for human GALT, 1295 bases in length, was established.
- The cDNA encodes a protein of approximately 43,000 Mr.
- The revised sequence indicates a higher degree of amino acid conservation between human GALT and its counterparts in Escherichia coli and yeast than previously recognized.
Conclusions:
- The revised human GALT cDNA sequence provides a more accurate genetic blueprint.
- Increased amino acid conservation suggests shared evolutionary origins and functional importance of GALT across species.
- This refined data aids in understanding GALT function and potential implications in metabolic studies.