[HTML][HTML] Binding of N-acetylglucosamine (GlcNAc) β1–6-branched oligosaccharide acceptors to β4-galactosyltransferase I reveals a new ligand binding mode

B Ramakrishnan, E Boeggeman, PK Qasba - Journal of Biological …, 2012 - ASBMB
N-Acetyllactosamine is the most prevalent disaccharide moiety in the glycans on the surface
of mammalian cells and often found as repeat units in the linear and branched …

Novel features of acceptor recognition by β-(1→ 4)-galactosyltransferase

Y Kajihara, H Kodama, T Endo, H Hashimoto - Carbohydrate research, 1998 - Elsevier
In order to understand how β-(1→ 4)-galactosyltransferase recognizes its glycosyl acceptor,
substrate specificities were investigated using synthetic 2-acetamido-2-deoxy-d …

Oligosaccharide preferences of β1, 4-galactosyltransferase-I: Crystal structures of Met340His mutant of human β1, 4-galactosyltransferase-I with a pentasaccharide …

V Ramasamy, B Ramakrishnan, E Boeggeman… - Journal of molecular …, 2005 - Elsevier
β-1, 4-Galactosyltransferase-I (β4Gal-T1) transfers galactose from UDP-galactose to N-
acetylglucosamine (GlcNAc) residues of the branched N-linked oligosaccharide chains of …

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 …

[HTML][HTML] Oligosaccharides Containing β1, 4-Linked N-Acetylgalactosamine, a Paradigm for Protein-specific Glycosylation (∗)

SM Manzella, LV Hooper, JU Baenziger - Journal of Biological Chemistry, 1996 - ASBMB
The carbohydrate moieties found on glycoproteins have long been recognized as having
great potential to bear biologically important information. However, actual examples of …

A novel variant form of murine β-1,6-N-acetylglucosaminyltransferase forming branches in poly-N-acetyllactosamines

GY Chen, N Kurosawa, T Muramatsu - Glycobiology, 2000 - academic.oup.com
A novel form of murine β-1, 6-N-acetylglucosaminyltransferase that forms branches in poly-N-
acetyllactosamines (designated as IGnT B) was cloned based on sequence homology to the …

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 …

Crystal structure of β1, 4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site

B Ramakrishnan, PV Balaji, PK Qasba - Journal of molecular biology, 2002 - Elsevier
The crystal structure of the catalytic domain of bovine β1, 4-galactosyltransferase (Gal-T1) co-
crystallized with UDP-Gal and MnCl2 has been solved at 2.8 Å resolution. The structure not …

Differential recognition of glycoprotein acceptors by terminal glycosyltransferases

J Yeh, RD Cummings - Glycobiology, 1997 - academic.oup.com
The factors regulating modifications of terminal β-Gal residues in lactosaminyl (Gaiβ→
4GlcNAcβ→ R) units in intact glycoproteins are not well understood. To examine these …

[HTML][HTML] Structure-based design of β1, 4-galactosyltransferase I (β4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens …

B Ramakrishnan, PK Qasba - Journal of Biological Chemistry, 2002 - ASBMB
β1, 4-Galactosyltransferase I (Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the
presence of Mn 2+ ion. In the presence of α-lactalbumin (LA), the Gal acceptor specificity is …