The vast number of proteins that sustain the currently living organisms have been generated
from a relatively small number of ancestral genes that has involved a variety of processes …

Galactosyltransferases are enzymes which transfer galactose from UDP-Gal to various
acceptors with either retention of the anomeric configuration to form α1, 2-, α1, 3-, α1, 4-, and …

Enzymatic glycosylation of proteins involves the addition of a monosaccharide or, in the
case of N-linked glycosylation of asparagine, a preformed oligosaccharide to an amino acid …

Abstract β1, 4‐galactosyltransferase T1 (β4Gal‐T1, EC 2.4. 1.90/38), a Golgi resident
membrane‐bound enzyme, transfers galactose from uridine diphosphogalactose to the …

BLAST analysis of expressed sequence tags (ESTs) using the coding sequence of the
human UDP-galactose: β-N-acetylglucosamine β1, 4-galactosyltransferase, designated …

Mucin-type O-glycosylation is initiated by a family of UDP-GalNAc: polypeptideN-
acetylgalactosaminyltransferases (ppGaNTases). Based on sequence relationships with …

Nomenclature EC number 2.7. 2.3 Systematic name ATP: 3-phospho-D-glycerate 1-
phosphotransferase Recommended name phosphoglycerate kinase Synonyms 3-PGK 3 …

The catalytic domain of bovine β1, 4-galactosyltransferase (β4Gal-T1) has been shown to
have two metal binding sites, each with a distinct binding affinity. Site I binds Mn2+ with high …

Abstract α1, 6-Fucosyltransferase catalyzes the transfer of fucose to the innermost GlcNAc
residue of an N-linked oligosaccharide. In order to identify the amino acid residue (s) which …

The enzyme β-1, 4-galactosyltransferase-1 (β4Gal-T1) catalyzes the transfer of a galactose
residue from UDP-Gal to the C4-hydroxyl group of N-acetylglucosamine. The catalytic …