Enzymatic synthesis of oligosaccharide analogues: UDP-Gal analogues as donors for three retaining alpha-galactosyltransferases

Authors
Sujino, K Uchiyama, T Hindsgaul, O Seto, NOL Wakarchuk, WW Palcic, MM
Citation
K. Sujino et al., Enzymatic synthesis of oligosaccharide analogues: UDP-Gal analogues as donors for three retaining alpha-galactosyltransferases, J AM CHEM S, 122(7), 2000, pp. 1261-1269
Citations number
59
Categorie Soggetti
Chemistry & Analysis",Chemistry
Journal title
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
ISSN journal
00027863 → ACNP
Volume
122
Issue
7
Year of publication
2000
Pages
1261 - 1269
Database
ISI
SICI code
0002-7863(20000223)122:7<1261:ESOOAU>2.0.ZU;2-6
Abstract
A series of deoxygenated uridine 5'-diphosphogalactose (UDP-Gal) derivative s are evaluated as donors for three different retaining galactosyltransfera ses using capillary electrophoresis with laser-induced fluorescence detecti on. The enzymes investigated were calf thymus alpha(1-->3) galactosyltransf erase (E.C. 2.4.1.151), blood group B alpha(1-->3) galactosyltransferase (E .C. 2.4.1.37) and Neisseria meningitidis alpha(1-->4) galactosyltransferase . UDP-2-deoxy-Gal and UDP-6-deoxy-Gal were found to be active as donors for all three enzymes. Preparative syntheses utilizing these UDP-Gal derivativ es were performed on mg scales, affording deoxygenated trisaccharide analog ues in 5-100% yields.