Disease relevance of galT

• We describe the molecular cloning of the gal operon of Salmonella typhimurium LT2 and the localization of the gal promoter and the genes galE, galT, and galK [1].
• A fusion enzyme consisting of UDP-galactose 4-epimerase and galactose-1-P uridylyltransferase with an intervening Ala3 linker was constructed by in-frame fusion of E. coli gene galT to the 3'-terminus of the E. coli gene galE that had been extended with the coding sequence for three alanine residues, all contained within a high-expression plasmid [2].
• By complementing appropriate gal lesions in Escherichia coli K802, we were able to isolate the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes of Lactobacillus helveticus [3].
• The isolation of restriction fragments containing the primary and secondary (galT) bacterial att sites of phage lambda [4].
• Downstream of and overlapping with the alpha-galactosidase genes of both strains, a gene was identified that is similar to the galactose-1-phosphate uridylyltransferase gene (galT) of E. coli and Streptomyces lividans [5].

High impact information on galT

• DNA sequences of portions of the wild-type galT gene which act as the target sites for these insertions, as well as the corresponding gal/IS1 junctions, are reported [6].
• Recombinant E. coli that overexpress the UDP-Gal biosynthetic genes galT, galK, and galU were generated [7].
• This promoter directs transcription of the galT, galE, and galK genes [8].
• Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine [9].
• Galactose-1-phosphate uridylyltransferase (GalT) catalyzes the reversible transformation of uridine 5'-diphosphate glucose (UDPGlc) and galactose-1-phosphate into uridine 5'-diphosphate galactose (UDPGal) and glucose-1-phosphate through a double displacement mechanism, with the intermediate formation of a covalent uridylyl-enzyme (UMP-enzyme) [9].

Chemical compound and disease context of galT

• The galT gene of Escherichia coli, which codes for the uridylyltransferase and is contained in a plasmid for transformation of E. coli, has been sequenced, and the positions of the 15 histidine residues have been determined from the deduced amino acid sequence of this protein [10].

Biological context of galT

• We constructed a plasmid that contained a defined 0.4-kilobase deletion in the galE but still expressed galT and galK activities from the gal promoter [1].
• The function of the galE gene but not of the galT or galK gene is required for bacterial virulence on pear fruits and seedlings [11].
• Three mutations caused by the integration of IS4 in galT in both possible orientations were shown by DNA sequence analysis to be integrated between a duplication of eleven base pairs of gene galT [12].
• Xanthomonas campestris pv. campestris, which displays no significant beta-1,4-D-galactopyranosidase activity, has three annotated beta-galactosidase genes in the sequenced genome, designated galA, galB and galC herein [13].

Associations of galT with chemical compounds

• Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site [14].
• Galactose-1-phosphate uridylyltransferase catalyzes the reaction of UDP-glucose with galactose 1-phosphate to form UDP-galactose and glucose 1-phosphate during normal cellular metabolism [15].
• Galactose-1-phosphate uridylyltransferase catalyzes the reversible transfer of the uridine 5'-monophosphoryl moiety of UDP-glucose to the phosphate group of galactose 1-phosphate to form UDP-galactose [16].
• The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer [15].
• Galactose-1-phosphate uridylyltransferase (GalT) catalyzes the reversible transformation of UDP-glucose and galactose-1-phosphate (Gal-1-P) into UDP-galactose and glucose-1-phosphate (Glc-1-P) by a double displacement mechanism, with the intermediate formation of a covalent uridylyl-enzyme (UMP-enzyme) [17].

Analytical, diagnostic and therapeutic context of galT

• Galactose-1-phosphate uridylyltransferase: identification of histidine-164 and histidine-166 as critical residues by site-directed mutagenesis [10].
• Crystallization and preliminary crystallographic analysis of galactose-1-phosphate uridylyltransferase from Escherichia coli [18].

References