A model of photoprobe docking with β1, 4-galactosyltransferase identifies a possible carboxylate involved in glycosylation steps
Y Hatanaka, M Ishiguro, M Hashimoto… - Bioorganic & medicinal …, 2001 - Elsevier
A molecular docking study has been performed on the interaction of β1, 4-
galactosyltransferase with an acceptor site photoprobe. This is based on an acceptor site …
galactosyltransferase with an acceptor site photoprobe. This is based on an acceptor site …
Identification of photolabeled peptides for the acceptor substrate binding domain of β1, 4-galactosyltransferase
M Hashimoto, Y Hatanaka - Chemical and pharmaceutical bulletin, 1999 - jstage.jst.go.jp
抄録 We successfully applied a carbene-generating N-acetylglucosamine derivative carrying
a biotinyl group to the radioisotope-free identification of peptides within bovine UDP …
a biotinyl group to the radioisotope-free identification of peptides within bovine UDP …
Structure and catalytic cycle of β-1, 4-galactosyltransferase
B Ramakrishnan, E Boeggeman, V Ramasamy… - Current opinion in …, 2004 - Elsevier
β-1, 4-galactosyltransferase-1, a housekeeping enzyme that functions in the synthesis of
glycoconjugates, has two flexible loops, one short and one long. Upon binding a metal ion …
glycoconjugates, has two flexible loops, one short and one long. Upon binding a metal ion …
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 …
Structure of bovine α‐1, 3‐galactosyltransferase and its complexes with UDP and DPGal inferred from molecular modeling
M Rao, I Tvaroska - Proteins: Structure, Function, and …, 2001 - Wiley Online Library
A homology model of α‐1, 3‐galactosyltransferase (α‐1, 3‐GalT), the retaining enzyme
responsible for the formation of α‐galactosyl epitopes, has been developed by means of …
responsible for the formation of α‐galactosyl epitopes, has been developed by means of …
Crystal structures of β-1, 4-galactosyltransferase 7 enzyme reveal conformational changes and substrate binding
Y Tsutsui, B Ramakrishnan, PK Qasba - Journal of Biological Chemistry, 2013 - ASBMB
The β-1, 4-galactosyltransferase 7 (β4GalT7) enzyme is involved in proteoglycan synthesis.
In the presence of a manganese ion, it transfers galactose from UDP-galactose to xylose on …
In the presence of a manganese ion, it transfers galactose from UDP-galactose to xylose on …
[HTML][HTML] Crystal structures of the bovine β4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
LN Gastinel, C Cambillau, Y Bourne - The EMBO Journal, 1999 - embopress.org
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 …
membrane‐bound enzyme, transfers galactose from uridine diphosphogalactose to the …
The role of tryptophan 314 in the conformational changes of β1, 4-galactosyltransferase-I
V Ramasamy, B Ramakrishnan, E Boeggeman… - Journal of molecular …, 2003 - Elsevier
β1, 4-Galactosyltransferase-I (β4Gal-T1) undergoes critical conformational changes upon
substrate binding from an open conformation (conf-I) to the closed conformation (conf-II) …
substrate binding from an open conformation (conf-I) to the closed conformation (conf-II) …
Interdependence of backbone flexibility, residue conservation, and enzyme function: A case study on β1, 4-galactosyltransferase-I
K Gunasekaran, B Ma, B Ramakrishnan, PK Qasba… - Biochemistry, 2003 - ACS Publications
β1, 4-Galactosyltransferase-I (β4Gal-T1) catalyzes the transfer of a galactose from UDP-
galactose to N-acetylglucosamine. A recent crystal structure determination of the substrate …
galactose to N-acetylglucosamine. A recent crystal structure determination of the substrate …
Active site studies of bovine α1→ 3-galactosyltransferase and its secondary structure prediction
The catalytic domain of bovine α1→ 3-galactosyltransferase (α3GalT), residues 80–368,
have been cloned and expressed, in Escherichia coli. Using a sequential purification …
have been cloned and expressed, in Escherichia coli. Using a sequential purification …