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Michael Schalli - One of the best experts on this subject based on the ideXlab platform.
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a new type of pharmacological chaperone for gm1 gangliosidosis related human lysosomal β galactosidase n substituted 5 amino 1 hydroxymethyl cyclopentanetriols
Bioorganic & Medicinal Chemistry Letters, 2017Co-Authors: Michael Schalli, Patrick Weber, Christina Tysoe, Bettina M Pabst, Martin Thonhofer, Eduard Paschke, Arnold E Stutz, Marion Tschernutter, Werner Windischhofer, Stephen G WithersAbstract:Abstract N -Functionalized amino(hydroxymethyl)cyclopentanetriols are potent inhibitors of β- d -Galactosidases and, for the first time, could be shown to act as pharmacological chaperones for G M1 -gangliosidosis-associated lysosomal acid β-galactosidase thus representing a new structural type of pharmacological chaperones for this lysosomal storage disease.
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n substituted 5 amino 1 hydroxymethyl cyclopentanetriols a new family of activity promotors for a gm1 gangliosidosis related human lysosomal β galactosidase mutant
Carbohydrate Research, 2017Co-Authors: Michael Schalli, Christina Tysoe, Bettina M Pabst, Martin Thonhofer, Eduard Paschke, Arnold E Stutz, Marion Tschernutter, Roland Fischer, Tanja Rappitsch, Werner WindischhoferAbstract:Abstract From 1,2;3,4-di-O-isopropylidene-α-D-galactopyranose, a series of highly functionalized (hydroxymethyl)cyclopentanes was easily available. In line with reports by Reymond and Jager on similar structures, these amine containing basic carbasugars are potent inhibitors of β-D-Galactosidases and, for the first time, could be shown to act as pharmacological chaperones for GM1-gangliosidosis-associated lysosomal acid β-galactosidase mutant R201C, thus representing a new structural type of pharmacological chaperones for this lysosomal storage disease.
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c 5a substituted validamine type glycosidase inhibitors
Carbohydrate Research, 2017Co-Authors: Michael Schalli, Christina Tysoe, Martin Thonhofer, Arnold E Stutz, Roland Fischer, Andreas Wolfsgruber, Andres G Santana, Stephen G WithersAbstract:A series of N-alkyl derivatives of the D-galactosidase inhibitor 1,4-di-epi-validamine featuring lipophilic substituents at position C-5a was prepared and screened for their glycosidase inhibitory properties. Products turned out selective for β-Galactosidases as well as β-glucosidases.
Werner Windischhofer - One of the best experts on this subject based on the ideXlab platform.
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a new type of pharmacological chaperone for gm1 gangliosidosis related human lysosomal β galactosidase n substituted 5 amino 1 hydroxymethyl cyclopentanetriols
Bioorganic & Medicinal Chemistry Letters, 2017Co-Authors: Michael Schalli, Patrick Weber, Christina Tysoe, Bettina M Pabst, Martin Thonhofer, Eduard Paschke, Arnold E Stutz, Marion Tschernutter, Werner Windischhofer, Stephen G WithersAbstract:Abstract N -Functionalized amino(hydroxymethyl)cyclopentanetriols are potent inhibitors of β- d -Galactosidases and, for the first time, could be shown to act as pharmacological chaperones for G M1 -gangliosidosis-associated lysosomal acid β-galactosidase thus representing a new structural type of pharmacological chaperones for this lysosomal storage disease.
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n substituted 5 amino 1 hydroxymethyl cyclopentanetriols a new family of activity promotors for a gm1 gangliosidosis related human lysosomal β galactosidase mutant
Carbohydrate Research, 2017Co-Authors: Michael Schalli, Christina Tysoe, Bettina M Pabst, Martin Thonhofer, Eduard Paschke, Arnold E Stutz, Marion Tschernutter, Roland Fischer, Tanja Rappitsch, Werner WindischhoferAbstract:Abstract From 1,2;3,4-di-O-isopropylidene-α-D-galactopyranose, a series of highly functionalized (hydroxymethyl)cyclopentanes was easily available. In line with reports by Reymond and Jager on similar structures, these amine containing basic carbasugars are potent inhibitors of β-D-Galactosidases and, for the first time, could be shown to act as pharmacological chaperones for GM1-gangliosidosis-associated lysosomal acid β-galactosidase mutant R201C, thus representing a new structural type of pharmacological chaperones for this lysosomal storage disease.
Stephen G Withers - One of the best experts on this subject based on the ideXlab platform.
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a new type of pharmacological chaperone for gm1 gangliosidosis related human lysosomal β galactosidase n substituted 5 amino 1 hydroxymethyl cyclopentanetriols
Bioorganic & Medicinal Chemistry Letters, 2017Co-Authors: Michael Schalli, Patrick Weber, Christina Tysoe, Bettina M Pabst, Martin Thonhofer, Eduard Paschke, Arnold E Stutz, Marion Tschernutter, Werner Windischhofer, Stephen G WithersAbstract:Abstract N -Functionalized amino(hydroxymethyl)cyclopentanetriols are potent inhibitors of β- d -Galactosidases and, for the first time, could be shown to act as pharmacological chaperones for G M1 -gangliosidosis-associated lysosomal acid β-galactosidase thus representing a new structural type of pharmacological chaperones for this lysosomal storage disease.
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c 5a substituted validamine type glycosidase inhibitors
Carbohydrate Research, 2017Co-Authors: Michael Schalli, Christina Tysoe, Martin Thonhofer, Arnold E Stutz, Roland Fischer, Andreas Wolfsgruber, Andres G Santana, Stephen G WithersAbstract:A series of N-alkyl derivatives of the D-galactosidase inhibitor 1,4-di-epi-validamine featuring lipophilic substituents at position C-5a was prepared and screened for their glycosidase inhibitory properties. Products turned out selective for β-Galactosidases as well as β-glucosidases.
Valeria Monteze Guimaraes - One of the best experts on this subject based on the ideXlab platform.
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purification and characterization of aspergillus terreus α Galactosidases and their use for hydrolysis of soymilk oligosaccharides
Applied Biochemistry and Biotechnology, 2011Co-Authors: Joana Gasperazzo Ferreira, Valeria Monteze Guimaraes, Angelica Pataro Reis, Daniel Luciano Falkoski, Lilian Da Silva Fialho, Sebastiao Tavares De RezendeAbstract:α-Galactosidases has the potential to hydrolyze α-1-6 linkages in raffinose family oligosaccharides (RFO). Aspergillus terreus cells cultivated on wheat bran produced three extracellular forms of α-Galactosidases (E1, E2, and E3). E1 and E2 α-Galactosidases presented maximal activities at pH 5, while E3 α-galactosidase was more active at pH 5.5. The E1 and E2 enzymes showed stability for 6 h at pH 4–7. Maximal activities were determined at 60, 55, and 50°C, for E1, E2, and E3 α-galactosidase, respectively. E2 α-galactosidase retained 90% of its initial activity after 70 h at 50°C. The enzymes hydrolyzed ρNPGal, melibiose, raffinose and stachyose, and E1 and E2 enzymes were able to hydrolyze guar gum and locust bean gum substrates. E1 and E3 α-Galactosidases were completely inhibited by Hg2+, Ag+, and Cu2+. The treatment of RFO present in soy milk with the enzymes showed that E1 α-galactosidase reduced the stachyose content to zero after 12 h of reaction, while E2 promoted total hydrolysis of raffinose. The complete removal of the oligosaccharides in soy milk could be reached by synergistic action of both enzymes
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debaryomyces hansenii ufv 1 intracellular α galactosidase characterization and comparative studies with the extracellular enzyme
Journal of Agricultural and Food Chemistry, 2009Co-Authors: Pollyanna Amaral Viana, Sebastiao Tavares De Rezende, Flavia Maria Lopes Passos, Marcelo P Bemquerer, Jamil S Oliveira, Kadima N Teixeira, Alexandre Martins Costa Santos, Jose C Rosa, Marcelo M Santoro, Valeria Monteze GuimaraesAbstract:Debaryomyces hansenii cells cultivated on galactose produced extracellular and intracellular alpha-Galactosidases, which showed 54.5 and 54.8 kDa molecular mass (MALDI-TOF), 60 and 61 kDa (SDS-PAGE) and 5.15 and 4.15 pI values, respectively. The extracellular and intracellular deglycosylated forms presented 36 and 40 kDa molecular mass, with 40 and 34% carbohydrate content, respectively. The N-terminal sequences of the alpha-Galactosidases were identical. Intracellular alpha-galactosidase showed smaller thermostability when compared to the extracellular enzyme. D. hansenii UFV-1 extracellular alpha-galactosidase presented higher kcat than the intracellular enzyme (7.16 vs 3.29 s-1, respectively) for the p-nitrophenyl-alpha-D-galactopyranoside substrate. The Km for hydrolysis of pNPalphaGal, melibiose, stachyose, and raffinose were 0.32, 2.12, 10.8, and 32.8 mM, respectively. The intracellular enzyme was a competitively inhibited by galactose (Ki = 0.70 mM), and it was inactivated by Cu(II) and Ag(I). Enzyme incubation with soy milk for 6 h at 55 degrees C reduced stachyose and raffinose amounts by 100 and 73%, respectively.
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hydrolysis of oligosaccharides in soybean products by debaryomyces hansenii ufv 1 α Galactosidases
Food Chemistry, 2007Co-Authors: Pollyanna Amaral Viana, Sebastiao Tavares De Rezende, Daniel Luciano Falkoski, Thiago De Almeida Leite, Ines Charnel Jose, Maurilio Alves Moreira, Valeria Monteze GuimaraesAbstract:α-Galactosides are abundant sugars found in legumes such as soybean. Since humans and monogastric animals lack α-galactosidase in the digestive tract, they are unable to digest these sugars, which induce flatulence. The use of α-Galactosidases is promising as a means to overcome this problem, and to increase the consumption of soy products. Immobilized α-galactosidase, derived from Debaryomyces hansenii UFV-1, exhibited an activity of 40 U per g of silica and an activity yield of 50%. The optimum pH of free and immobilized α-galactosidase was 5.0 and the optima temperatures were 60 and 80 °C, respectively. The soymilk stachyose was completely hydrolyzed by different enzyme forms after incubation for 4 h at 60 °C, while raffinose was reduced by 100%, 25% and 68% by free, immobilized enzymes and permeabilized cells, respectively. The soy molasses treatment with free enzyme for 6 h promoted reduction in stachyose and raffinose contents by 100% and 50%, respectively.
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processing of soybean products by semipurified plant and microbial α Galactosidases
Journal of Agricultural and Food Chemistry, 2006Co-Authors: Daniel Luciano Falkoski, Valeria Monteze Guimaraes, Angelica Pataro Reis, Carina Marin Callegari, Everaldo Goncalves De Barros, Sebastiao Tavares De RezendeAbstract:Galactooligosaccharides (GO) are responsible for intestinal disturbances following ingestion of legume-derived products. Enzymatic reduction of GO level in these products is highly desirable to improve their acceptance. For this purpose, plant and microbial semipurified α-Galactosidases were used for GO hydrolysis in soybean flour and soy molasses. α-Galactosidases from soybean germinating seeds, Aspergillus terreus, and Penicillium griseoroseum presented maximal activities at pH 4.0−5.0 and 45−65 °C. The KM,app values determined for raffinose by the soybean, A. terreus, and P. griseoroseum α-Galactosidases were 3.44, 19.39, and 20.67 mM, respectively. The enzymes were completely inhibited by Ag+ and Hg2+, whereas only soybean enzyme was inhibited by galactose. A. terreus α-galactosidase was more thermostable than the enzymes from the other two sources. This enzyme maintained about 100% of its original activity after 3 h at 60 °C. The microbial α-Galactosidases were more efficient for reducing GO in soybe...
Christina Tysoe - One of the best experts on this subject based on the ideXlab platform.
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a new type of pharmacological chaperone for gm1 gangliosidosis related human lysosomal β galactosidase n substituted 5 amino 1 hydroxymethyl cyclopentanetriols
Bioorganic & Medicinal Chemistry Letters, 2017Co-Authors: Michael Schalli, Patrick Weber, Christina Tysoe, Bettina M Pabst, Martin Thonhofer, Eduard Paschke, Arnold E Stutz, Marion Tschernutter, Werner Windischhofer, Stephen G WithersAbstract:Abstract N -Functionalized amino(hydroxymethyl)cyclopentanetriols are potent inhibitors of β- d -Galactosidases and, for the first time, could be shown to act as pharmacological chaperones for G M1 -gangliosidosis-associated lysosomal acid β-galactosidase thus representing a new structural type of pharmacological chaperones for this lysosomal storage disease.
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n substituted 5 amino 1 hydroxymethyl cyclopentanetriols a new family of activity promotors for a gm1 gangliosidosis related human lysosomal β galactosidase mutant
Carbohydrate Research, 2017Co-Authors: Michael Schalli, Christina Tysoe, Bettina M Pabst, Martin Thonhofer, Eduard Paschke, Arnold E Stutz, Marion Tschernutter, Roland Fischer, Tanja Rappitsch, Werner WindischhoferAbstract:Abstract From 1,2;3,4-di-O-isopropylidene-α-D-galactopyranose, a series of highly functionalized (hydroxymethyl)cyclopentanes was easily available. In line with reports by Reymond and Jager on similar structures, these amine containing basic carbasugars are potent inhibitors of β-D-Galactosidases and, for the first time, could be shown to act as pharmacological chaperones for GM1-gangliosidosis-associated lysosomal acid β-galactosidase mutant R201C, thus representing a new structural type of pharmacological chaperones for this lysosomal storage disease.
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c 5a substituted validamine type glycosidase inhibitors
Carbohydrate Research, 2017Co-Authors: Michael Schalli, Christina Tysoe, Martin Thonhofer, Arnold E Stutz, Roland Fischer, Andreas Wolfsgruber, Andres G Santana, Stephen G WithersAbstract:A series of N-alkyl derivatives of the D-galactosidase inhibitor 1,4-di-epi-validamine featuring lipophilic substituents at position C-5a was prepared and screened for their glycosidase inhibitory properties. Products turned out selective for β-Galactosidases as well as β-glucosidases.
