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Cloning and characterization of a cDNA encoding human galactose-1-phosphate uridyl transferase.
Department of Biochemistry, Stanford University School of Medicine, CA 94305.
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.
PMID: 2840550 [PubMed - indexed for MEDLINE]
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Cited by 11 PubMed Central articles
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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.
[Biosci Hypotheses. 2008]
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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.
[Biochemistry. 2002]
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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.
[Proc Natl Acad Sci U S A. 1996]
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