Identification of a UDP-Gal:beta-galactoside beta 1----3-galactosyltransferase in the albumen gland of the snail Lymnaea stagnalis.
Detergent extracts of the albumen gland of the snail Lymnaea stagnalis contain an enzyme activity that transfers Gal from UDP-Gal to acceptor substrates with terminal non-reducing beta-galactose residues. The products formed with lactose (Gal beta 1----4Glc) as the acceptor were characterized by HPLC, and subjected to 400-MHz 1H-NMR and methylation analysis. The main product was shown to have the structure Gal beta 1----3Gal beta 1----4Glc. Therefore, the galactosyltransferase can be identified as a UDP-Gal:beta-galactoside beta 1----3-galactosyltransferase. In view of its linkage and acceptor specificity, the enzyme may be essential to the biosynthesis of galactogen, the main polysaccharide produced by albumen glands of L. stagnalis.
D000818:Animals; D005088:Exocrine Glands / Q000201:enzymology; D005260:Female; D005685:Galactans / Q000096:biosynthesis; D005690:Galactose / Q000378:metabolism; D005700:Galactosyltransferases / Q000378:metabolism*; D007785:Lactose / Q000378:metabolism; D008195:Lymnaea / Q000201:enzymology*; D013379:Substrate Specificity; D014531:Uridine Diphosphate Galactose / Q000378:metabolism
D005685:Galactans; D014531:Uridine Diphosphate Galactose; C007812:galactogen; D005700:Galactosyltransferases; C053604:UDP-Gal-beta-galactoside beta1-3-galactosyltransferase; D007785:Lactose; D005690:Galactose