Mol Biol Med. 1988 Apr;5(2):107-22.

Cloning and characterization of a cDNA encoding human galactose-1-phosphate uridyl transferase.

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Department of Biochemistry, Stanford University School of Medicine, CA 94305.

Abstract

We report the cloning and characterization of a cDNA that encodes a functional human galactose-1-phosphate uridyl transferase (GALT). The cDNA is 1400 bases in length and encodes a 43,000 Mr protein. The cloning strategy involved the identification of short peptide sequences conserved between the homologous enzymes from Escherichia coli and yeast, and the construction of oligonucleotide pools corresponding to the conserved patches. These patches of conserved amino acids tend to be conserved in humans as well.

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Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase. [Mol Biol Med. 1990]
Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase.
Flach JE, Reichardt JK, Elsas LJ 2nd. Mol Biol Med. 1990 Aug; 7(4):365-9.
Galactose utilization in Lactobacillus helveticus: isolation and characterization of the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes. [J Bacteriol. 1991]
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Review The yeast, Saccharomyces cerevisiae, as a model system for the study of human genetic disease.
Wells L, Fridovich-Keil JL. SAAS Bull Biochem Biotechnol. 1996; 9:83-8.
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Cited by 11 PubMed Central articles

ARHI: A new target of galactose toxicity in Classic Galactosemia. [Biosci Hypotheses. 2008]
ARHI: A new target of galactose toxicity in Classic Galactosemia.
Lai K, Tang M, Yin X, Klapper H, Wierenga K, Elsas L. Biosci Hypotheses. 2008; 1(5):263-271.
Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. [Biochemistry. 2002]
Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases.
Brenner C. Biochemistry. 2002 Jul 23; 41(29):9003-14.
Heterodimer formation and activity in the human enzyme galactose-1-phosphate uridylyltransferase. [Proc Natl Acad Sci U S A. 1996]
Heterodimer formation and activity in the human enzyme galactose-1-phosphate uridylyltransferase.
Elsevier JP, Wells L, Quimby BB, Fridovich-Keil JL. Proc Natl Acad Sci U S A. 1996 Jul 9; 93(14):7166-71.

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Mol Biol Med. 1988 Apr ;5(2):107-22.

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Cloning and characterization of a cDNA encoding human galactose-1-phosphate uridyl transferase.

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