Structural analysis of milk and testis beta-1,4-galactosyltransferase gene products.
There seems to exist a relatively low similarity between the amino acid sequences of the testis and milk beta-1,4-galactosyltransferase gene products. However, the predicted higher structures of testis and milk beta-1,4-galactosyltransferase proteins revealed a highly significant similarity in the regions required for enzymatic activities. Testis beta-1,4-galactosyltransferase protein contained a WD repeat similar to the motif of the G protein beta subunit type I and a Zn-finger motif at the N- and C-terminal portions of the protein, respectively. Phylogenetic analysis of glycosyltransferase proteins revealed that the ancestral gene of testis and milk beta-1,4-galactosyltransferases and alpha-1,3-galactosyltransferase evolved into three different destinations at about the same time on an evolutionary scale.
Uehara
K
K
First Department of Biochemistry, Nagoya University School of Medicine, Japan.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002645:Chickens; D019143:Evolution, Molecular; D005700:Galactosyltransferases / Q000737:chemistry*; D006801:Humans; D008297:Male; D051379:Mice; D008892:Milk / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009237:N-Acetyllactosamine Synthase / Q000737:chemistry*; D010802:Phylogeny; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D013737:Testis / Q000201:enzymology*
D005700:Galactosyltransferases; C037959:beta-D-galactosyl-N-acetylglucosaminylglycopeptide alpha-1,3-galactosyltransferase; D009237:N-Acetyllactosamine Synthase