UDP-N-Acetyl-α-D-glucosamine as acceptor substrate of β-1, 4-galactosyltransferase. Enzymatic synthesis of UDP-N-acetyllactosamine

L Elling, A Zervosen, R Gutiérrez Gallego… - Glycoconjugate …, 1999 - Springer
The capacity of UDP-N-acetyl-α-D-glucosamine (UDP-GlcNAc) as an in vitro acceptor
substrate for β-1, 4-galactosyltransferase (β4GalT1, EC 2.4. 1.38) from human and bovine …

Differences in N-acetyllactosamine synthesis between β-1, 4-galactosyltransferases I and V

T Sato, K Furukawa - Glycoconjugate journal, 1999 - Springer
Abstract Unlike classical β-1, 4-galactosyltransferase (β-1, 4-GalT I), β-1, 4-GalT V (formerly
IV*) has little activity towards 1 mM N-acetylglucosamine [Sato et al.(1998) Proc Natl Acad …

Chemical synthesis and kinetic characterization of UDP-2-deoxy-d-lyxo-hexose (“UDP-2-deoxy-d-galactose”), a donor-substrate for β-(1→ 4)-d-galactosyltransferase

G Srivastava, O Hindsgaul, MM Palcic - Carbohydrate research, 1993 - Elsevier
Abstract Bovine β-(1→ 4)-galactosyltransferase (GalT) transfers galactose from UDP-
galactose to β-d-GlcpNAc-terminating oligosaccharides to produce N-acetyllactosamine …

Characterization of the substrate specificity of α1, 3galactosyltransferase utilizing modified N-acetyllactosamine disaccharides

CLM Stults, BA Macher, R Bhatti, OP Srivastava… - …, 1999 - academic.oup.com
Abstract α1, 3galactosyltransferase (α1, 3GalT) catalyzes the synthesis of a range of
glycoconjugates containing the Galα1, 3Gal epitope which is recognized by the naturally …

Recombinant Soluble β‐1,4‐Galactosyltransferases Expressed in Saccharomyces cerevisiae Purification, Characterization and Comparison with Human Enzyme

M Malissard, L Borsig, S Di Marco… - European journal of …, 1996 - Wiley Online Library
β‐1, 4‐Galactosyltransferase (Gal‐T, EC 2.4. 1.38) transfers galactose (Gal) from JDP‐Gal to
N‐acetyl‐d‐glucosamine or a derivative GlcNAc‐R. Soluble Gal‐T, purified from human …

Production and characterization of active soluble human β1, 4-galactosyltransferase in Escherichia coli as a useful catalyst in synthesis of the Gal β1→ 4 GlcNAc …

S Shibatani, K Fujiyama, S Nishiguchi, T Seki… - Journal of bioscience …, 2001 - Elsevier
An active and soluble human β1, 4-galactosyltransferase (β-GT) was produced in
Escherichia coli using a maltose-binding protein fusion system. The purified recombinant β …

Flexibility in the donor substrate specificity of β 1,4-galactosyltransferase: application in the synthesis of complex carbohydrates

MM Palcic, O Hindsgaul - Glycobiology, 1991 - academic.oup.com
Biosynthetically, bovine N-acetylglucosainine β 1, 4-galacto-syltransferase (GalT) catalyses
the transfer of galactosyl residues from UDP-Gal to the 4-position of GlcNAc units, resulting …

[HTML][HTML] Genomic cloning and expression of three murine UDP-galactose: β-N-acetylglucosamine β1, 3-galactosyltransferase genes

T Hennet, A Dinter, P Kuhnert, TS Mattu… - Journal of Biological …, 1998 - ASBMB
Based on the detection of expressed sequence tags that are similar to known
galactosyltransferase sequences, we have isolated three novel UDP-galactose: β-N …

Investigations on β1, 4-galactosyltransferase I using 6-sulfo-GlcNAc as an acceptor sugar substrate

B Ramakrishnan, AJ Moncrief, TA Davis… - Glycoconjugate …, 2013 - Springer
sulfate modified N-acetylglucosamine (6-sulfo-GlcNAc) is often found as part of many
biologically important carbohydrate epitopes such as 6-sulfo-Le X. In these epitopes, the 6 …

Occurrence of poly-N-acetyllactosamine synthesis in Sf-9 cells upon transfection of individual human β-1, 4-galactosyltransferase I, II, III, IV, V and VI cDNAs

T Sato, S Guo, K Furukawa - Biochimie, 2001 - Elsevier
Lectin blot analysis of membrane glycoprotein samples from Sf-9 cells upon transfection of
individual human β-1, 4-galactosyltransferase (β-1, 4-GalT) I, II, III, IV, V et VI cDNAs showed …