Enzymatic α(1→2)-l-fucosylation: investigation of the specificity of the α(1→2)-l-galactosyltransferase from Helix pomatia

✍ Scribed by Angela Michelle Scheppokat; Minoru Morita; Joachim Thiem; Hagen Bretting

• Book ID: 104359994
• Publisher: Elsevier Science
• Year: 2003
• Tongue: English
• Weight: 213 KB
• Volume: 14
• Category: Article
• ISSN: 0957-4166
• DOI: 10.1016/s0957-4166(03)00521-4

✦ Synopsis

The a(12)-L-galactosyltransferase from Helix pomatia transfers an L-fucosyl residue from GDP-L-Fucose to a terminal, non-reducing D-galactopyranosyl moiety of an oligosaccharide. The extent of the enzyme's specificity towards the stereochemistry at the D-galactopyranosyl anomeric centre, the site of interglycosidic linkage and the nature of the subterminal oligosaccharide residue has been investigated using HPAEC-PAD and MALDI-TOF technology. This a(12)-L-galactosyltransferase is specific for D-galactopyranosyl b-linkages, independent of the site of the interglycosidic linkage and aglycone configuration and with limited specificity for the nature of the subterminal sugar residue.