[HTML][HTML] An acceptor analogue of β-1, 4-galactosyltransferase: Substrate, inhibitor, or both?
J Jiang, GK Wagner - Carbohydrate research, 2017 - Elsevier
Many glycosyltransferase inhibitors in the literature are structurally derived from the donor or
acceptor substrate of the respective enzyme. A representative example is 2-naphthyl β-d …
acceptor substrate of the respective enzyme. A representative example is 2-naphthyl β-d …
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 …
crystallized with UDP-Gal and MnCl2 has been solved at 2.8 Å resolution. The structure not …
β3-galactosyltransferase-V
H Narimatsu - Handbook of Glycosyltransferases and Related Genes, 2002 - Springer
Abstract β3-Galactosyltransferase (β3GalT) transfers a galactose from UDP-Gal to N-
acetylglucosamine (GlcNAc) with a β1, 3-linkage. To date, five members of the β3GalT family …
acetylglucosamine (GlcNAc) with a β1, 3-linkage. To date, five members of the β3GalT family …
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 …
the transfer of galactosyl residues from UDP-Gal to the 4-position of GlcNAc units, resulting …
[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 …
presence of Mn 2+ ion. In the presence of α-lactalbumin (LA), the Gal acceptor specificity is …
[HTML][HTML] The dimeric structure of wild-type human glycosyltransferase B4GalT1
D Harrus, F Khoder-Agha, M Peltoniemi, A Hassinen… - PLoS …, 2018 - journals.plos.org
Most glycosyltransferases, including B4GalT1 (EC 2.4. 1.38), are known to assemble into
enzyme homomers and functionally relevant heteromers in vivo. However, it remains …
enzyme homomers and functionally relevant heteromers in vivo. However, it remains …
[HTML][HTML] Probing the acceptor active site organization of the human recombinant β1, 4-galactosyltransferase 7 and design of xyloside-based inhibitors
M Saliba, N Ramalanjaona, S Gulberti… - Journal of Biological …, 2015 - ASBMB
Among glycosaminoglycan (GAG) biosynthetic enzymes, the human β1, 4-
galactosyltransferase 7 (hβ4GalT7) is characterized by its unique capacity to take over …
galactosyltransferase 7 (hβ4GalT7) is characterized by its unique capacity to take over …
UDP-Gal: GlcNAc-R β1, 4-galactosyltransferase—a target enzyme for drug design. Acceptor specificity and inhibition of the enzyme
I Brockhausen, M Benn, S Bhat, S Marone… - Glycoconjugate …, 2006 - Springer
Galactosyltransferases are important enzymes for the extension of the glycan chains of
glycoproteins and glycolipids, and play critical roles in cell surface functions and in the …
glycoproteins and glycolipids, and play critical roles in cell surface functions and in the …
Galactosyltransferases: a structural overview of their function and reaction mechanisms
LN Gastinel - Trends in Glycoscience and Glycotechnology, 2001 - jstage.jst.go.jp
抄録 ガラクトース転移酵素は糖転移酵素のファミリーの中で最も代表的なものである.
ガラクトース転移酵素は UDP-α-D-ガラクトースを供与体としてガラクトースを糖タンパク質 …
ガラクトース転移酵素は UDP-α-D-ガラクトースを供与体としてガラクトースを糖タンパク質 …
Characterization and synthetic application of a novel β1, 3-galactosyltransferase from Escherichia coli O55: H7
A β1, 3-galactosyltransferase (WbgO) was identified in Escherichia coli O55: H7. Its function
was confirmed by radioactive activity assay and structure analysis of the disaccharide …
was confirmed by radioactive activity assay and structure analysis of the disaccharide …