-
1
-
-
0024431691
-
Glycosyltransferases - structure, localization, and control of cell type-specific glycosylation
-
Paulson JC, Colley KJ Glycosyltransferases - structure, localization, and control of cell type-specific glycosylation. J Biol Chem. 264:1989;17614-17618.
-
(1989)
J Biol Chem
, vol.264
, pp. 17614-17618
-
-
Paulson, J.C.1
Colley, K.J.2
-
2
-
-
0344706380
-
A family of human β4-galactosyltransferases: Cloning and expression of two novel UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferases, β4Gal-T2 and β4Gal-T3
-
Almeida R, Amado M, David L, Levery SB, Holmes EH, Merkx G, van Kessel AG, Rygaard E, Hassan H, Bennett E, Clausen H A family of human β4-galactosyltransferases: cloning and expression of two novel UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferases, β4Gal-T2 and β4Gal-T3. J Biol Chem. 272:1997;31979-31991.
-
(1997)
J Biol Chem
, vol.272
, pp. 31979-31991
-
-
Almeida, R.1
Amado, M.2
David, L.3
Levery, S.B.4
Holmes, E.H.5
Merkx, G.6
Van Kessel, A.G.7
Rygaard, E.8
Hassan, H.9
Bennett, E.10
Clausen, H.11
-
3
-
-
0031930477
-
Molecular cloning of a human cDNA encoding β-1,4-galactosyltransferase with 37% identity to mammalian UDP-Gal:GlcNAc β-1,4-galactosyltransferase
-
Sato T, Furukawa K, Bakker H, van den Eijnden DH, van Die I Molecular cloning of a human cDNA encoding β-1,4-galactosyltransferase with 37% identity to mammalian UDP-Gal:GlcNAc β-1,4-galactosyltransferase. Proc Natl Acad Sci USA. 95:1998;472-477.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 472-477
-
-
Sato, T.1
Furukawa, K.2
Bakker, H.3
Van Den Eijnden, D.H.4
Van Die, I.5
-
4
-
-
0032491511
-
Cloning of a novel member of the UDP-Galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis
-
Schwientek T, Almeida R, Levery SB, Holmes EH, Bennett E, Clausen H Cloning of a novel member of the UDP-Galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J Biol Chem. 273:1998;29331-29340.
-
(1998)
J Biol Chem
, vol.273
, pp. 29331-29340
-
-
Schwientek, T.1
Almeida, R.2
Levery, S.B.3
Holmes, E.H.4
Bennett, E.5
Clausen, H.6
-
5
-
-
15644371731
-
Purification, cDNA cloning, and expression of UDP-Gal:glucosylceramide β-1,4-galactosyltransferase from rat brain
-
Nomura T, Takizawa M, Aoki J, Arai H, Inoue K, Wakisaka E, Yoshizuba N, Imokawa G, Dohmae N, Takio Ket al. Purification, cDNA cloning, and expression of UDP-Gal:glucosylceramide β-1,4-galactosyltransferase from rat brain. J Biol Chem. 273:1998;13570-13577.
-
(1998)
J Biol Chem
, vol.273
, pp. 13570-13577
-
-
Nomura, T.1
Takizawa, M.2
Aoki, J.3
Arai, H.4
Inoue, K.5
Wakisaka, E.6
Yoshizuba, N.7
Imokawa, G.8
Dohmae, N.9
Takio, K.10
-
6
-
-
0032567431
-
Synthesis of poly-N-acetyllactosamine in core 2 branched O-glycans: The requirement of novel β-1,4-galactosyltransferase IV and β-1,3-N-acetylglucosaminyltransferase
-
Ujita M, McAuliffe J, Schwientek T, Almeida R, Hindsgaul O, Clausen H, Fukuda M Synthesis of poly-N-acetyllactosamine in core 2 branched O-glycans: the requirement of novel β-1,4-galactosyltransferase IV and β-1,3-N-acetylglucosaminyltransferase. J Biol Chem. 273:1998;34843-34849.
-
(1998)
J Biol Chem
, vol.273
, pp. 34843-34849
-
-
Ujita, M.1
McAuliffe, J.2
Schwientek, T.3
Almeida, R.4
Hindsgaul, O.5
Clausen, H.6
Fukuda, M.7
-
7
-
-
0031469691
-
Identification of conserved amino acid motifs in members of the β1-4-galactosyltransferase gene family
-
van Die I, Bakker H, van den Eijnden DH Identification of conserved amino acid motifs in members of the β1-4-galactosyltransferase gene family. Glycobiology. 7:1997;v-ix.
-
(1997)
Glycobiology
, vol.7
-
-
Van Die, I.1
Bakker, H.2
Van Den Eijnden, D.H.3
-
8
-
-
0031777054
-
The expanding β4-galactosyltransferase gene family: Messages from the databanks
-
Lo NW, Shaper JH, Pevsner J, Shaper NL The expanding β4-galactosyltransferase gene family: messages from the databanks. Glycobiology. 8:1998;517-526.
-
(1998)
Glycobiology
, vol.8
, pp. 517-526
-
-
Lo, N.W.1
Shaper, J.H.2
Pevsner, J.3
Shaper, N.L.4
-
9
-
-
0032478833
-
CDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetyl galactosaminyltransferase sequence homologs from Caenorhabditis elegans
-
Hagen FK, Nehrke K cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetyl galactosaminyltransferase sequence homologs from Caenorhabditis elegans. J Biol Chem. 273:1998;8268-8277.
-
(1998)
J Biol Chem
, vol.273
, pp. 8268-8277
-
-
Hagen, F.K.1
Nehrke, K.2
-
10
-
-
0032906430
-
Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
-
Several conserved motifs have been defined for each fucosyltransferase group. A general model for the evolution of fucosyltransferases, by successive duplications followed by divergent evolution from one or two ancestral genes, is proposed.
-
Oriol R, Mollicone R, Cailleau A, Balanzino L, Breton C Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria. Glycobiology. 9:1999;323-334. Several conserved motifs have been defined for each fucosyltransferase group. A general model for the evolution of fucosyltransferases, by successive duplications followed by divergent evolution from one or two ancestral genes, is proposed.
-
(1999)
Glycobiology
, vol.9
, pp. 323-334
-
-
Oriol, R.1
Mollicone, R.2
Cailleau, A.3
Balanzino, L.4
Breton, C.5
-
11
-
-
3543040594
-
Molecular cloning and characterization of an α1,3fucosyltransferase, CEFT-1, from Caenorhabditis elegans
-
DeBose-Boyd RA, Nyame AK, Cummings RD Molecular cloning and characterization of an α1,3fucosyltransferase, CEFT-1, from Caenorhabditis elegans. Glycobiology. 8:1998;905-917.
-
(1998)
Glycobiology
, vol.8
, pp. 905-917
-
-
Debose-Boyd, R.A.1
Nyame, A.K.2
Cummings, R.D.3
-
12
-
-
0032955846
-
Expression of three Caenorhabditis elegans N-acetylglucosaminyltransferase I genes during development
-
Although only a single copy of the GnT-I (N-acetylglucosaminyltransferase I) gene has been reported to date in mammals, three genes that show significant homology to mammalian GnT-I have been identified in the C. elegans genome. Two of them were shown to encode active GnT-I. The third one is either inactive or could exhibit a new, uncharacterized specificity.
-
Chen S, Zhou S, Sarkar M, Spence AM, Schachter H Expression of three Caenorhabditis elegans N-acetylglucosaminyltransferase I genes during development. J Biol Chem. 274:1999;288-297. Although only a single copy of the GnT-I (N-acetylglucosaminyltransferase I) gene has been reported to date in mammals, three genes that show significant homology to mammalian GnT-I have been identified in the C. elegans genome. Two of them were shown to encode active GnT-I. The third one is either inactive or could exhibit a new, uncharacterized specificity.
-
(1999)
J Biol Chem
, vol.274
, pp. 288-297
-
-
Chen, S.1
Zhou, S.2
Sarkar, M.3
Spence, A.M.4
Schachter, H.5
-
13
-
-
0030851778
-
Lewis X biosynthesis in Helicobacter pylori: Molecular cloning of an α(1,3)fucosyltransferase gene
-
Martin SL, Edbrooke MR, Hodgman TC, van den Eijnden DH, Bird MI Lewis X biosynthesis in Helicobacter pylori: molecular cloning of an α(1,3)fucosyltransferase gene. J Biol Chem. 272:1997;21349-21356.
-
(1997)
J Biol Chem
, vol.272
, pp. 21349-21356
-
-
Martin, S.L.1
Edbrooke, M.R.2
Hodgman, T.C.3
Van Den Eijnden, D.H.4
Bird, M.I.5
-
14
-
-
0030851782
-
Cloning and heterologous expression of an α1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori
-
Ge Z, Chan NWC, Palcic MM, Taylor DE Cloning and heterologous expression of an α1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori. J Biol Chem. 272:1997;21357-21363.
-
(1997)
J Biol Chem
, vol.272
, pp. 21357-21363
-
-
Ge, Z.1
Chan, N.W.C.2
Palcic, M.M.3
Taylor, D.E.4
-
16
-
-
0031086055
-
Identification of two novel conserved amino acid residues in eukaryotic sialyltransferases: Implications for their mechanism of action
-
Geremia RA, Harduin-Lepers A, Delannoy P Identification of two novel conserved amino acid residues in eukaryotic sialyltransferases: implications for their mechanism of action. Glycobiology. 7:1997;V.
-
(1997)
Glycobiology
, vol.7
-
-
Geremia, R.A.1
Harduin-Lepers, A.2
Delannoy, P.3
-
17
-
-
0029961489
-
Cloning of the lipooligosaccharide α-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae
-
Gilbert M, Watson DC, Cunningham AM, Jennings MP, Young NM, Wakarchuk WW Cloning of the lipooligosaccharide α-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae. J Biol Chem. 271:1996;28271-28276.
-
(1996)
J Biol Chem
, vol.271
, pp. 28271-28276
-
-
Gilbert, M.1
Watson, D.C.2
Cunningham, A.M.3
Jennings, M.P.4
Young, N.M.5
Wakarchuk, W.W.6
-
18
-
-
0031913180
-
Cloning and expression of a marine β-galactoside α2,6-sialyltransferase gene from Photobacterium damsela JT0160
-
Yamamoto T, Nakashizuka M, Terada I Cloning and expression of a marine β-galactoside α2,6-sialyltransferase gene from Photobacterium damsela JT0160. J Biochem. 123:1998;94-100.
-
(1998)
J Biochem
, vol.123
, pp. 94-100
-
-
Yamamoto, T.1
Nakashizuka, M.2
Terada, I.3
-
19
-
-
0028985664
-
The sialyltransferase 'sialylmotif' participates in binding the donor substrate CMP-NeuAc
-
Datta AK, Paulson JC The sialyltransferase 'sialylmotif' participates in binding the donor substrate CMP-NeuAc. J Biol Chem. 270:1995;1497-1500.
-
(1995)
J Biol Chem
, vol.270
, pp. 1497-1500
-
-
Datta, A.K.1
Paulson, J.C.2
-
20
-
-
0032540299
-
Mutation of the sialyltransferase S-sialylmotif alters the kinetics of the donor and acceptor substrates
-
m values for both donor and acceptor substrates.
-
m values for both donor and acceptor substrates.
-
(1998)
J Biol Chem
, vol.273
, pp. 9608-9614
-
-
Datta, A.K.1
Sinha, A.2
Paulson, J.C.3
-
21
-
-
0027467841
-
A conserved disulphide bond in sialyltransferases
-
Drickamer K A conserved disulphide bond in sialyltransferases. Glycobiology. 3:1993;2-3.
-
(1993)
Glycobiology
, vol.3
, pp. 2-3
-
-
Drickamer, K.1
-
22
-
-
0031909680
-
Conserved structural features in eukaryotic and prokaryotic fucosyltransferases
-
Breton C, Oriol R, Imberty A Conserved structural features in eukaryotic and prokaryotic fucosyltransferases. Glycobiology. 8:1998;87-94.
-
(1998)
Glycobiology
, vol.8
, pp. 87-94
-
-
Breton, C.1
Oriol, R.2
Imberty, A.3
-
23
-
-
0032566438
-
Human α1,3/4-fucosyltransferases. III-A Lys/Arg residue located within the α1,3-FucT motif is required for activity but not substrate binding
-
m values, of either substrate.
-
m values, of either substrate.
-
(1998)
J Biol Chem
, vol.273
, pp. 25256-25260
-
-
Sherwood, A.L.1
Nguyen, A.T.2
Whitaker, J.M.3
MacHer, B.A.4
Stroud, M.R.5
Holmes, E.H.6
-
24
-
-
0029736391
-
Mechanism and specificity of human α1,3-fucosyltransferase V
-
Murray BW, Takayama S, Schultz J, Wong CH Mechanism and specificity of human α1,3-fucosyltransferase V. Biochemistry. 35:1996;11183-11195.
-
(1996)
Biochemistry
, vol.35
, pp. 11183-11195
-
-
Murray, B.W.1
Takayama, S.2
Schultz, J.3
Wong, C.H.4
-
25
-
-
0031749203
-
Sequence function relationships of prokaryotic and eukaryotic galactosyltransferases
-
An extensive sequence analysis of all the known galactosyltransferases and related proteins led to the definition of five families and to the identification of a common motif (DxD) in all but one of the families.
-
Breton C, Bettler E, Joziasse DH, Geremia R, Imberty A Sequence function relationships of prokaryotic and eukaryotic galactosyltransferases. J Biochem. 123:1998;1000-1009. An extensive sequence analysis of all the known galactosyltransferases and related proteins led to the definition of five families and to the identification of a common motif (DxD) in all but one of the families.
-
(1998)
J Biochem
, vol.123
, pp. 1000-1009
-
-
Breton, C.1
Bettler, E.2
Joziasse, D.H.3
Geremia, R.4
Imberty, A.5
-
26
-
-
0032493440
-
Activity of the yeast MNN1 α-1,3 mannosyltransferase requires a motif conserved in many other families of glycosyltransferases
-
•], in several glycosyltransferase families and demonstrate that it is essential for MNN1 (α3-ManT) enzyme activity.
-
•], in several glycosyltransferase families and demonstrate that it is essential for MNN1 (α3-ManT) enzyme activity.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 7945-7950
-
-
Wiggins, C.A.R.1
Munro, S.2
-
27
-
-
0344628712
-
Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase - essential residues lie in a predicted active site cleft resembling a lactose repressor fold
-
Using both theoretical and experimental approaches, the authors propose a new model for the catalytic domain of polypeptide:N-acetylgalactosaminyltransferase and demonstrate the importance of the most conserved histidine and acidic amino acid residues in enzyme function. None of the mutations in the C-terminal lectin-like domain alters the catalytic properties of ppGalNAcT1
-
Hagen FK, Hazes B, Raffo R, deSa D, Tabak LA Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase - essential residues lie in a predicted active site cleft resembling a lactose repressor fold. J Biol Chem. 274:1999;6797-6803. Using both theoretical and experimental approaches, the authors propose a new model for the catalytic domain of polypeptide:N-acetylgalactosaminyltransferase and demonstrate the importance of the most conserved histidine and acidic amino acid residues in enzyme function. None of the mutations in the C-terminal lectin-like domain alters the catalytic properties of ppGalNAcT1.
-
(1999)
J Biol Chem
, vol.274
, pp. 6797-6803
-
-
Hagen, F.K.1
Hazes, B.2
Raffo, R.3
Desa, D.4
Tabak, L.A.5
-
28
-
-
0030664369
-
Identification of essential residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1
-
Wragg S, Hagen FK, Tabak LA Identification of essential residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1. Biochem J. 328:1997;193-197.
-
(1997)
Biochem J
, vol.328
, pp. 193-197
-
-
Wragg, S.1
Hagen, F.K.2
Tabak, L.A.3
-
29
-
-
0032584665
-
A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins
-
•], is essential to enzyme activity and that it probably participates in the coordination of the metal cation during the binding of UDP-glucose.
-
•], is essential to enzyme activity and that it probably participates in the coordination of the metal cation during the binding of UDP-glucose.
-
(1998)
J Biol Chem
, vol.273
, pp. 19566-19572
-
-
Busch, C.1
Hofmann, F.2
Selzer, J.3
Munro, S.4
Jeckel, D.5
Aktories, K.6
-
30
-
-
0033083847
-
Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli
-
The blood group A (α3-GalNAcT) and B (α3-GalT) glycosyltransferases differ at only four positions. Kinetic measurements of a series of hybrid A-B enzymes demonstrate the importance of a single amino acid change (Leu266Met) in determining the A versus B donor specificity. In addition, A-B transferases were shown to be able to use other nucleotide donors, such as UDP-GlcNAc and UDP-Glc.
-
Seto NOL, Compston CA, Evans SV, Bundle DR, Narang SA, Palcic MM Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli. Eur J Biochem. 259:1999;770-775. The blood group A (α3-GalNAcT) and B (α3-GalT) glycosyltransferases differ at only four positions. Kinetic measurements of a series of hybrid A-B enzymes demonstrate the importance of a single amino acid change (Leu266Met) in determining the A versus B donor specificity. In addition, A-B transferases were shown to be able to use other nucleotide donors, such as UDP-GlcNAc and UDP-Glc.
-
(1999)
Eur J Biochem
, vol.259
, pp. 770-775
-
-
Seto, N.O.L.1
Compston, C.A.2
Evans, S.V.3
Bundle, D.R.4
Narang, S.A.5
Palcic, M.M.6
-
31
-
-
0029097304
-
Human α(1,3/1,4)-fucosyltransferases discriminate between different oligosaccharide acceptor substrates through a discrete peptide segment
-
Legault DJ, Kelly RJ, Natsuka Y, Lowe JB Human α(1,3/1,4)-fucosyltransferases discriminate between different oligosaccharide acceptor substrates through a discrete peptide segment. J Biol Chem. 270:1995;20987-20996.
-
(1995)
J Biol Chem
, vol.270
, pp. 20987-20996
-
-
Legault, D.J.1
Kelly, R.J.2
Natsuka, Y.3
Lowe, J.B.4
-
32
-
-
0029988870
-
Structure-function analysis of human α1-3-fucosyltransferases. Amino acids involved in acceptor substrate specificity
-
Xu Z, Vo L, Macher BA Structure-function analysis of human α1-3-fucosyltransferases. Amino acids involved in acceptor substrate specificity. J Biol Chem. 271:1996;8818-8823.
-
(1996)
J Biol Chem
, vol.271
, pp. 8818-8823
-
-
Xu, Z.1
Vo, L.2
MacHer, B.A.3
-
33
-
-
0033617436
-
A single amino acid in the hypervariable stem domain of vertebrate α1,3/1,4-fucosyltransferases determines the type 1/type 2 transfer: Characterization of acceptor substrate specificity of the Lewis enzyme by site-directed mutagenesis
-
An elegant study demonstrating that a single amino acid change (Trp111Arg) in the Lewis enzyme (FucT-III), which uses almost exclusively type 1 acceptor (Galβ1,3GlcNAc), is sufficient to change the specificity of fucose transfer to type 2 acceptor (Galβ1,4GlcNAc). In contrast, the 'inverse' mutation (Arg115Trp) in FucT-b, which has a strict specificity for type 2 acceptor, leads to an inactive enzyme for both types of acceptors.
-
Dupuy F, Petit JM, Mollicone R, Oriol R, Julien R, Maftah A A single amino acid in the hypervariable stem domain of vertebrate α1,3/1,4-fucosyltransferases determines the type 1/type 2 transfer: characterization of acceptor substrate specificity of the Lewis enzyme by site-directed mutagenesis. J Biol Chem. 274:1999;12257-12262. An elegant study demonstrating that a single amino acid change (Trp111Arg) in the Lewis enzyme (FucT-III), which uses almost exclusively type 1 acceptor (Galβ1,3GlcNAc), is sufficient to change the specificity of fucose transfer to type 2 acceptor (Galβ1,4GlcNAc). In contrast, the 'inverse' mutation (Arg115Trp) in FucT-b, which has a strict specificity for type 2 acceptor, leads to an inactive enzyme for both types of acceptors.
-
(1999)
J Biol Chem
, vol.274
, pp. 12257-12262
-
-
Dupuy, F.1
Petit, J.M.2
Mollicone, R.3
Oriol, R.4
Julien, R.5
Maftah, A.6
-
34
-
-
0032566436
-
Human α1,3/4-fucosyltransferases. II- A single amino acid at the COOH terminus of FucT III and V alters their kinetic properties
-
Vo L, Lee S, Marcinko MC, Holmes EH, Macher BA Human α1,3/4-fucosyltransferases. II- A single amino acid at the COOH terminus of FucT III and V alters their kinetic properties. J Biol Chem. 273:1998;25250-25255.
-
(1998)
J Biol Chem
, vol.273
, pp. 25250-25255
-
-
Vo, L.1
Lee, S.2
Marcinko, M.C.3
Holmes, E.H.4
MacHer, B.A.5
-
35
-
-
0027965664
-
Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
-
Vrielink A, Ruger W, Driessen HP, Freemont PS Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J. 13:1994;3413-3422.
-
(1994)
EMBO J
, vol.13
, pp. 3413-3422
-
-
Vrielink, A.1
Ruger, W.2
Driessen, H.P.3
Freemont, P.S.4
-
37
-
-
0028969335
-
Evolutionary link between glycogen phosphorylase and a DNA modifying enzyme
-
Holm L, Sander C Evolutionary link between glycogen phosphorylase and a DNA modifying enzyme. EMBO J. 14:1995;1287-1293.
-
(1995)
EMBO J
, vol.14
, pp. 1287-1293
-
-
Holm, L.1
Sander, C.2
-
38
-
-
0033580656
-
Structure of the nucleotide-diphospho sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms
-
The SpsA enzyme is implicated in the biosynthesis of the spore coat. Its donor and acceptor specificities are unknown, but part of its sequence is related to cellulose synthase and bacterial polysaccharide synthases. The 1.5 Å resolution three-dimensional structure of the native and complexed enzyme gave information both on the active site and on the recognition mode for the nucleotide moiety of the donor.
-
Charnok SJ, Davies GJ Structure of the nucleotide-diphospho sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry. 38:1999;6380-6385. The SpsA enzyme is implicated in the biosynthesis of the spore coat. Its donor and acceptor specificities are unknown, but part of its sequence is related to cellulose synthase and bacterial polysaccharide synthases. The 1.5 Å resolution three-dimensional structure of the native and complexed enzyme gave information both on the active site and on the recognition mode for the nucleotide moiety of the donor.
-
(1999)
Biochemistry
, vol.38
, pp. 6380-6385
-
-
Charnok, S.J.1
Davies, G.J.2
-
39
-
-
0033168184
-
Crystal structures of the bovine β4-galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose
-
••]. Most similarities are displayed in the nucleotide-binding region, whereas the putative acceptor domain presents more differences.
-
••]. Most similarities are displayed in the nucleotide-binding region, whereas the putative acceptor domain presents more differences.
-
(1999)
EMBO J
, vol.18
, pp. 3546-3557
-
-
Gastinel, L.N.1
Cambillau, C.2
Bourne, Y.3
-
40
-
-
0032777708
-
Fold recognition study of α3-galactosyltransferase and molecular modeling of the nucleotide sugar-binding domain
-
A bioinformatic and molecular modeling study of pig α3-GalT, the enzyme responsible for the biosynthesis of the xenotransplantation antigen. The nucleotide-sugar-binding domain is predicted to adopt a Rossmann fold, similar to the one observed in phage T4 β-GlcT. Both UDP-galactose and a divalent cation are included in the final model.
-
Imberty A, Monier C, Bettler E, Morera S, Freemont P, Sippl M, Flöckner H, Rüger W, Breton C Fold recognition study of α3-galactosyltransferase and molecular modeling of the nucleotide sugar-binding domain. Glycobiology. 9:1999;713-722. A bioinformatic and molecular modeling study of pig α3-GalT, the enzyme responsible for the biosynthesis of the xenotransplantation antigen. The nucleotide-sugar-binding domain is predicted to adopt a Rossmann fold, similar to the one observed in phage T4 β-GlcT. Both UDP-galactose and a divalent cation are included in the final model.
-
(1999)
Glycobiology
, vol.9
, pp. 713-722
-
-
Imberty, A.1
Monier, C.2
Bettler, E.3
Morera, S.4
Freemont, P.5
Sippl, M.6
Flöckner, H.7
Rüger, W.8
Breton, C.9
-
41
-
-
0031404510
-
Fold recognition and molecular modeling of a lectin-like domain in UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases
-
Imberty A, Piller V, Piller F, Breton C Fold recognition and molecular modeling of a lectin-like domain in UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Protein Eng. 10:1997;1353-1356.
-
(1997)
Protein Eng
, vol.10
, pp. 1353-1356
-
-
Imberty, A.1
Piller, V.2
Piller, F.3
Breton, C.4
-
42
-
-
0345588683
-
T4 phage β-glucosyltransferase: substrate binding and proposed catalytic mechanism
-
in press
-
Moréra S, Imberty A, Aschke-Sonnenbron U, Rüger W, Freemont P: T4 phage β-glucosyltransferase: substrate binding and proposed catalytic mechanism. J Mol Biol 1999, in press.
-
(1999)
J Mol Biol
-
-
Moréra, S.1
Imberty, A.2
Aschke-Sonnenbron, U.3
Rüger, W.4
Freemont, P.5
-
43
-
-
0031039932
-
Mechanism of human α1,3-fucosyltransferase V: Glycosidic cleavage occurs prior to nucleophilic attack
-
Murray BW, Wittmann V, Burkart MD, Hung SC, Wong CH Mechanism of human α1,3-fucosyltransferase V: glycosidic cleavage occurs prior to nucleophilic attack. Biochemistry. 36:1997;823-831.
-
(1997)
Biochemistry
, vol.36
, pp. 823-831
-
-
Murray, B.W.1
Wittmann, V.2
Burkart, M.D.3
Hung, S.C.4
Wong, C.H.5
-
44
-
-
0033054563
-
Selective inhibition of β-1,4- And α-1,3-galactosyltransferases: Donor sugar-nucleotide based approach
-
Identified using rational design, 56 potential inhibitors of β4-GalT were screened using electrospray mass spectrometry. It was demonstrated that the pyrophosphate portion is crucial for inhibition and also that this inhibition is metal-dependent. Galactose-type 1-N-imino sugar is identified as a new inhibitor of α3-GalT. Possible mechanisms of reaction are proposed for both β4-GalT and α3-GalT.
-
Takayama S, Chung SJ, Igarashi Y, Ichikawa Y, Sepp A, Lechler RI, Wu J, Hayashi T, Siuzdak G, Wong C-H Selective inhibition of β-1,4- and α-1,3-galactosyltransferases: donor sugar-nucleotide based approach. Bioorg Med Chem. 7:1999;401-409. Identified using rational design, 56 potential inhibitors of β4-GalT were screened using electrospray mass spectrometry. It was demonstrated that the pyrophosphate portion is crucial for inhibition and also that this inhibition is metal-dependent. Galactose-type 1-N-imino sugar is identified as a new inhibitor of α3-GalT. Possible mechanisms of reaction are proposed for both β4-GalT and α3-GalT.
-
(1999)
Bioorg Med Chem
, vol.7
, pp. 401-409
-
-
Takayama, S.1
Chung, S.J.2
Igarashi, Y.3
Ichikawa, Y.4
Sepp, A.5
Lechler, R.I.6
Wu, J.7
Hayashi, T.8
Siuzdak, G.9
Wong, C.-H.10
-
45
-
-
0030952095
-
Synthesis of the first tricomponent bisubstrate analogue that exhibits potent inhibition against GlcNAc:β-1,4-galactosyltransferase
-
Hashimoto H, Endo T, Kajihara Y Synthesis of the first tricomponent bisubstrate analogue that exhibits potent inhibition against GlcNAc:β-1,4-galactosyltransferase. J Org Chem. 62:1997;1914-1915.
-
(1997)
J Org Chem
, vol.62
, pp. 1914-1915
-
-
Hashimoto, H.1
Endo, T.2
Kajihara, Y.3
-
46
-
-
0032401126
-
Acceptor substrate-based selective inhibition of galactosyltransferases
-
Chung SJ, Takayama S, Wong CH Acceptor substrate-based selective inhibition of galactosyltransferases. Bioorg Med Chem. 8:1998;3359-3364.
-
(1998)
Bioorg Med Chem
, vol.8
, pp. 3359-3364
-
-
Chung, S.J.1
Takayama, S.2
Wong, C.H.3
-
47
-
-
0030669711
-
On the role of manganese cation in the mechanism of α-1,3-fucosyltransferase
-
Smith SL, Compston CA, Palcic MM, Bamford MJ, Britten CJ, Field RA On the role of manganese cation in the mechanism of α-1,3-fucosyltransferase. Biochem Soc Trans. 25:1997;S630.
-
(1997)
Biochem Soc Trans
, vol.25
, pp. 630
-
-
Smith, S.L.1
Compston, C.A.2
Palcic, M.M.3
Bamford, M.J.4
Britten, C.J.5
Field, R.A.6
-
48
-
-
0023657949
-
Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
-
Gaboriaud C, Bissery VL, Benchetrit T, Mornon JP Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 224:1987;149-155.
-
(1987)
FEBS Lett
, vol.224
, pp. 149-155
-
-
Gaboriaud, C.1
Bissery, V.L.2
Benchetrit, T.3
Mornon, J.P.4
|