Screening of recombinant glycosyltransferases reveals the broad acceptor specificity of stevia UGT-76G1

2016 ◽  
Vol 233 ◽  
pp. 49-55 ◽  
Author(s):  
Griet Dewitte ◽  
Maarten Walmagh ◽  
Margo Diricks ◽  
Alexander Lepak ◽  
Alexander Gutmann ◽  
...  
Keyword(s):  
Acceptor Specificity

Acceptor specificity and tissue distribution of three human alpha-3-fucosyltransferases

1990 ◽  
Vol 191 (1) ◽  
pp. 169-176 ◽  
Author(s):  
Rosella MOLLICONE ◽  
Anne GIBAUD ◽  
Anne FRANCOIS ◽  
Murray RATCLIFFE ◽  
Rafael ORIOL
Keyword(s):  
Tissue Distribution ◽  
Acceptor Specificity

Altering the Electron Acceptor Specificity of Flavocytochrome b2

1999 ◽  
Vol 27 (1) ◽  
pp. A45-A45
Author(s):  
Fraser Welsh ◽  
Stuart Rivers ◽  
Stephen K. Chapman ◽  
Graeme A. Reid
Keyword(s):  
Electron Acceptor ◽  
Flavocytochrome B2 ◽  
Acceptor Specificity

scholarly journals Acceptor Specificity of thePasteurellaHyaluronan and Chondroitin Synthases and Production of Chimeric Glycosaminoglycans

2006 ◽  
Vol 282 (1) ◽  
pp. 337-344 ◽  
Author(s):  
Breca S. Tracy ◽  
Fikri Y. Avci ◽  
Robert J. Linhardt ◽  
Paul L. DeAngelis
Keyword(s):  
Acceptor Specificity

scholarly journals A Combination of Structural, Genetic, Phenotypic and Enzymatic Analyses Reveals the Importance of a Predicted Fucosyltransferase to Protein O-Glycosylation in the Bacteroidetes

Biomolecules ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1795
Author(s):  
Markus B. Tomek ◽  
Bettina Janesch ◽  
Matthias L. Braun ◽  
Manfred Taschner ◽  
Rudolf Figl ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Mutational Analysis ◽  
Bacteroides Fragilis ◽  
Host Colonization ◽  
Acceptor Specificity ◽  
Hexose Sugars ◽  
Full Structure ◽  
Bacteroidetes Phylum ◽  
General Protein

Diverse members of the Bacteroidetes phylum have general protein O-glycosylation systems that are essential for processes such as host colonization and pathogenesis. Here, we analyzed the function of a putative fucosyltransferase (FucT) family that is widely encoded in Bacteroidetes protein O-glycosylation genetic loci. We studied the FucT orthologs of three Bacteroidetes species—Tannerella forsythia, Bacteroides fragilis, and Pedobacter heparinus. To identify the linkage created by the FucT of B. fragilis, we elucidated the full structure of its nine-sugar O-glycan and found that l-fucose is linked β1,4 to glucose. Of the two fucose residues in the T. forsythia O-glycan, the fucose linked to the reducing-end galactose was shown by mutational analysis to be l-fucose. Despite the transfer of l-fucose to distinct hexose sugars in the B. fragilis and T. forsythia O-glycans, the FucT orthologs from B. fragilis, T. forsythia, and P. heparinus each cross-complement the B. fragilis ΔBF4306 and T. forsythia ΔTanf_01305 FucT mutants. In vitro enzymatic analyses showed relaxed acceptor specificity of the three enzymes, transferring l-fucose to various pNP-α-hexoses. Further, glycan structural analysis together with fucosidase assays indicated that the T. forsythia FucT links l-fucose α1,6 to galactose. Given the biological importance of fucosylated carbohydrates, these FucTs are promising candidates for synthetic glycobiology.

scholarly journals Comparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites

2020 ◽  
pp. jbc.RA120.015305
Author(s):  
Renuka Kadirvelraj ◽  
Jeong-Yeh Yang ◽  
Hyun Woo Kim ◽  
Justin H. Sanders ◽  
Kelley W. Moremen ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Binding Site ◽  
Human Disease ◽  
Catalytic Mechanism ◽  
Substrate Recognition ◽  
Nucleotide Sugar ◽  
Modular Assembly ◽  
Acceptor Specificity ◽  
Donor Acceptor ◽  
Prior Models

Poly-N-acetyl-lactosamine (poly-LacNAc) structures are composed of repeating [-Galβ(1,4)-GlcNAcβ(1,3)-]n glycan extensions. They are found on both N- and O­-glycoproteins and glycolipids, and play an important role in development, immune function, and human disease. The majority of mammalian poly-LacNAc is synthesized by the alternating iterative action of β1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) and β1,4-galactosyltransferases. B3GNT2 is in the largest mammalian glycosyltransferase family, GT31, but little is known about the structure, substrate recognition, or catalysis by family members. Here we report the structures of human B3GNT2 in complex with UDP:Mg2+, and in complex with both UDP:Mg2+ and a glycan acceptor, lacto-N-neotetraose. The B3GNT2 structure conserves the GT-A fold and the DxD motif that coordinates a Mg2+ ion for binding the UDP-GlcNAc sugar donor. The acceptor complex shows interactions with only the terminal Galβ(1,4)-GlcNAcβ(1,3)- disaccharide unit, which likely explains the specificity for both N- and O-glycan acceptors. Modeling of the UDP-GlcNAc donor supports a direct displacement inverting catalytic mechanism. Comparative structural analysis indicates that nucleotide sugar donors for GT-A fold glycosyltransferases bind in similar positions and conformations without conserving interacting residues, even for enzymes that use the same donor substrate. In contrast, the B3GNT2 acceptor binding site is consistent with prior models suggesting that the evolution of acceptor specificity involves loops inserted into the stable GT-A fold. These observations support the hypothesis that GT-A fold glycosyltransferases employ co-evolving donor, acceptor, and catalytic subsite modules as templates to achieve the complex diversity of glycan linkages in biological systems.

Engineering the acceptor specificity of trehalose phosphorylase for the production of trehalose analogs

2012 ◽  
Vol 28 (5) ◽  
pp. 1257-1262 ◽  
Author(s):  
Jef Van der Borght ◽  
Wim Soetaert ◽  
Tom Desmet
Keyword(s):  
Acceptor Specificity ◽  
Trehalose Phosphorylase

scholarly journals The Acceptor Specificity of Amylomaltase from Escherichia coli IFO 3806

1989 ◽  
Vol 53 (10) ◽  
pp. 2661-2666 ◽  
Author(s):  
Sumio Kitahata ◽  
Hiromi Murakami ◽  
Yoshiaki Sone ◽  
Akira Misaki
Keyword(s):  
Escherichia Coli ◽  
Acceptor Specificity
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