The Experts below are selected from a list of 279 Experts worldwide ranked by ideXlab platform
Juan C. Ferrer - One of the best experts on this subject based on the ideXlab platform.
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Crystallization and preliminary X-ray analysis of the glycogen synthase from Pyrococcus abyssi.
Acta Crystallographica Section D-biological Crystallography, 2003Co-Authors: Cristina Horcajada, Emili Cid, Joan J. Guinovart, Núria Verdaguer, Juan C. FerrerAbstract:Glycogen synthase catalyzes the transfer of glucosyl residues from ADP- or UDP-glucose to the non-reducing end of a growing -1,4glucan chain. To date, no crystallographic structure of an animal/ fungal glycogen synthase (family 3 of the Glycosyl transferases) or a bacterial/plant glycogen/starch synthase (family 5) has been reported. This paper describes the recombinant expression, crystallization and preliminary X-ray analysis of the glycogen synthase from the hyperthermophilic archaeon Pyrococcus abyssi, the smallest enzyme of the members of families 3 and 5 of the Glycosyl transferases. Crystals from this protein and from its selenomethionyl variant were grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by the hanging-drop vapour-diffusion method at 293 K.
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Crystallization and preliminary X-ray analysis of the glycogen synthase from Pyrococcus abyssi.
Acta crystallographica. Section D Biological crystallography, 2003Co-Authors: Cristina Horcajada, Emili Cid, Joan J. Guinovart, Núria Verdaguer, Juan C. FerrerAbstract:Glycogen synthase catalyzes the transfer of glucosyl residues from ADP- or UDP-glucose to the non-reducing end of a growing alpha-1,4-glucan chain. To date, no crystallographic structure of an animal/fungal glycogen synthase (family 3 of the Glycosyl transferases) or a bacterial/plant glycogen/starch synthase (family 5) has been reported. This paper describes the recombinant expression, crystallization and preliminary X-ray analysis of the glycogen synthase from the hyperthermophilic archaeon Pyrococcus abyssi, the smallest enzyme of the members of families 3 and 5 of the Glycosyl transferases. Crystals from this protein and from its selenomethionyl variant were grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by the hanging-drop vapour-diffusion method at 293 K. The crystals, which grew as thin needles, diffracted to 3.5 A resolution and belong to space group C2, with unit-cell parameters a = 202, b = 73, c = 149 A, beta = 131 degrees. The crystallographic and biochemical data are consistent with either a dimer or a tetramer in the crystal asymmetric unit and a volume solvent content of 70 or 39%, respectively.
Cristina Horcajada - One of the best experts on this subject based on the ideXlab platform.
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Crystallization and preliminary X-ray analysis of the glycogen synthase from Pyrococcus abyssi.
Acta Crystallographica Section D-biological Crystallography, 2003Co-Authors: Cristina Horcajada, Emili Cid, Joan J. Guinovart, Núria Verdaguer, Juan C. FerrerAbstract:Glycogen synthase catalyzes the transfer of glucosyl residues from ADP- or UDP-glucose to the non-reducing end of a growing -1,4glucan chain. To date, no crystallographic structure of an animal/ fungal glycogen synthase (family 3 of the Glycosyl transferases) or a bacterial/plant glycogen/starch synthase (family 5) has been reported. This paper describes the recombinant expression, crystallization and preliminary X-ray analysis of the glycogen synthase from the hyperthermophilic archaeon Pyrococcus abyssi, the smallest enzyme of the members of families 3 and 5 of the Glycosyl transferases. Crystals from this protein and from its selenomethionyl variant were grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by the hanging-drop vapour-diffusion method at 293 K.
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Crystallization and preliminary X-ray analysis of the glycogen synthase from Pyrococcus abyssi.
Acta crystallographica. Section D Biological crystallography, 2003Co-Authors: Cristina Horcajada, Emili Cid, Joan J. Guinovart, Núria Verdaguer, Juan C. FerrerAbstract:Glycogen synthase catalyzes the transfer of glucosyl residues from ADP- or UDP-glucose to the non-reducing end of a growing alpha-1,4-glucan chain. To date, no crystallographic structure of an animal/fungal glycogen synthase (family 3 of the Glycosyl transferases) or a bacterial/plant glycogen/starch synthase (family 5) has been reported. This paper describes the recombinant expression, crystallization and preliminary X-ray analysis of the glycogen synthase from the hyperthermophilic archaeon Pyrococcus abyssi, the smallest enzyme of the members of families 3 and 5 of the Glycosyl transferases. Crystals from this protein and from its selenomethionyl variant were grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by the hanging-drop vapour-diffusion method at 293 K. The crystals, which grew as thin needles, diffracted to 3.5 A resolution and belong to space group C2, with unit-cell parameters a = 202, b = 73, c = 149 A, beta = 131 degrees. The crystallographic and biochemical data are consistent with either a dimer or a tetramer in the crystal asymmetric unit and a volume solvent content of 70 or 39%, respectively.
Matthieu Sollogoub - One of the best experts on this subject based on the ideXlab platform.
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From 1,4-Disaccharide to 1,3-Glycosyl Carbasugar: Synthesis of a Bespoke Inhibitor of Family GH99 Endo-α-mannosidase
Organic Letters, 2018Co-Authors: Sha Zhu, Lukasz Sobala, Ganeko Bernardo-seisdedos, Oscar Millet, Yongmin Zhang, Jesus Jimenez-barbero, Gideon Davies, Matthieu SollogoubAbstract:Understanding the enzyme reaction mechanism can lead to the design of enzyme inhibitors. A Claisen rearrangement was used to allow conversion of an α-1,4-disaccharide into an α-1,3-linked Glycosyl carbasugar to target the endo-α-mannosidase from the GH99 glycosidase family, which, unusually, is believed to act through a 1,2-anhydrosugar “epoxide” intermediate. Using NMR and X-ray crystallography, it is shown that glucosyl carbasugar α-aziridines can act as reasonably potent endo-α-mannosidase inhibitors, likely by virtue of their shape mimicry and the interactions of the aziridine nitrogen with the conserved catalytic acid/base of the enzyme active site.
Ping Liu - One of the best experts on this subject based on the ideXlab platform.
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Cycloartane triterpenes from Beesia calthaefolia and their anticomplement structure–activity relationship study
Journal of Asian natural products research, 2016Co-Authors: Jin-yuan Zhao, Jing Zhang, Ping LiuAbstract:Fifteen cycloartane triterpenes were isolated from Beesia calthaefolia and among them one was new cycloartane triterpenoid. The structure of new compound was determined by the application of spectroscopic analyses and chemical methods. The fifteen compounds were evaluated for their anticomplement activity by classic pathway. The structure-activity relationship analysis indicated that the configurations of 12-OH is preferable to be α than β, and 18-OH can decrease while 15-OH can increase the anticomplement activity, but saponin with both 15-OH and 18-OH lost most of its activity. The Glycosyl moiety of most isolated cycloartane triterpenes is xylosyl. When xylosyl was substituted by glucosyl or galactosyl, their anticomplement activities were decreased or increased, respectively. Further structure-activity relationship (SAR) studies must be carried out to achieve general conclusions regarding the effect of further functionalizations on the anticomplement saponins.
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cycloartane triterpenes from beesia calthaefolia and their anticomplement structure activity relationship study
Journal of Asian Natural Products Research, 2016Co-Authors: Jin-yuan Zhao, Jing Zhang, Ping LiuAbstract:Fifteen cycloartane triterpenes were isolated from Beesia calthaefolia and among them one was new cycloartane triterpenoid. The structure of new compound was determined by the application of spectroscopic analyses and chemical methods. The fifteen compounds were evaluated for their anticomplement activity by classic pathway. The structure-activity relationship analysis indicated that the configurations of 12-OH is preferable to be α than β, and 18-OH can decrease while 15-OH can increase the anticomplement activity, but saponin with both 15-OH and 18-OH lost most of its activity. The Glycosyl moiety of most isolated cycloartane triterpenes is xylosyl. When xylosyl was substituted by glucosyl or galactosyl, their anticomplement activities were decreased or increased, respectively. Further structure-activity relationship (SAR) studies must be carried out to achieve general conclusions regarding the effect of further functionalizations on the anticomplement saponins.
Emili Cid - One of the best experts on this subject based on the ideXlab platform.
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Crystallization and preliminary X-ray analysis of the glycogen synthase from Pyrococcus abyssi.
Acta Crystallographica Section D-biological Crystallography, 2003Co-Authors: Cristina Horcajada, Emili Cid, Joan J. Guinovart, Núria Verdaguer, Juan C. FerrerAbstract:Glycogen synthase catalyzes the transfer of glucosyl residues from ADP- or UDP-glucose to the non-reducing end of a growing -1,4glucan chain. To date, no crystallographic structure of an animal/ fungal glycogen synthase (family 3 of the Glycosyl transferases) or a bacterial/plant glycogen/starch synthase (family 5) has been reported. This paper describes the recombinant expression, crystallization and preliminary X-ray analysis of the glycogen synthase from the hyperthermophilic archaeon Pyrococcus abyssi, the smallest enzyme of the members of families 3 and 5 of the Glycosyl transferases. Crystals from this protein and from its selenomethionyl variant were grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by the hanging-drop vapour-diffusion method at 293 K.
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Crystallization and preliminary X-ray analysis of the glycogen synthase from Pyrococcus abyssi.
Acta crystallographica. Section D Biological crystallography, 2003Co-Authors: Cristina Horcajada, Emili Cid, Joan J. Guinovart, Núria Verdaguer, Juan C. FerrerAbstract:Glycogen synthase catalyzes the transfer of glucosyl residues from ADP- or UDP-glucose to the non-reducing end of a growing alpha-1,4-glucan chain. To date, no crystallographic structure of an animal/fungal glycogen synthase (family 3 of the Glycosyl transferases) or a bacterial/plant glycogen/starch synthase (family 5) has been reported. This paper describes the recombinant expression, crystallization and preliminary X-ray analysis of the glycogen synthase from the hyperthermophilic archaeon Pyrococcus abyssi, the smallest enzyme of the members of families 3 and 5 of the Glycosyl transferases. Crystals from this protein and from its selenomethionyl variant were grown in 100 mM sodium citrate pH 5.6 containing 20% PEG and 20% dioxane by the hanging-drop vapour-diffusion method at 293 K. The crystals, which grew as thin needles, diffracted to 3.5 A resolution and belong to space group C2, with unit-cell parameters a = 202, b = 73, c = 149 A, beta = 131 degrees. The crystallographic and biochemical data are consistent with either a dimer or a tetramer in the crystal asymmetric unit and a volume solvent content of 70 or 39%, respectively.
