The human galactose-1-phosphate uridyltransferase gene

• Published in: Genomics (San Diego, Calif.) Vol. 14; no. 2; p. 474
• Main Authors: Leslie, N D, Immerman, E B, Flach, J E, Florez, M, Fridovich-Keil, J L, Elsas, L J
• Format: Journal Article
• Language: English
• Published: United States 01-10-1992
• Subjects: Amino Acid Sequence; Base Sequence; Cell Line; DNA; Galactosemias - genetics; Humans; Molecular Sequence Data; Mutation; Polymerase Chain Reaction; Restriction Mapping; Sequence Homology, Amino Acid; UTP-Hexose-1-Phosphate Uridylyltransferase - genetics
• ISSN: 0888-7543
• DOI: 10.1016/S0888-7543(05)80244-7

Classical galactosemia is an inborn error of metabolism caused by a deficiency of galactose-1-phosphate uridyltransferase (GALT). Standard treatment with dietary galactose restriction will reverse the potentially lethal symptoms of the disease that are manifest in the newborn period. However, the long-term prognosis for these patients is variable. As a first step toward investigating the molecular basis for phenotypic variation in galactosemia, we have cloned and sequenced the entire gene for human galactose-1-phosphate uridyltransferase. This gene is organized into 11 exons spanning 4 kb. In exons 6, 9, and a portion of 10, there is a high degree of amino acid sequence conservation among Escherichia coli, yeast, mouse, and human. We have identified a number of nucleotide changes in the GALT genes of galactosemic patients that alter conserved amino acids. The most common of these is an A to G transition at nucleotide position 1470, converting a glutamine to an arginine at amino acid codon position 188 (Q188R).