Zobrazeno 1 - 10 of 13 pro vyhledávání: '"Christiane Goedl"'
1
Substitution of the catalytic acid–base Glu237 by Gln suppresses hydrolysis during glucosylation of phenolic acceptors catalyzed by Leuconostoc mesenteroides sucrose phosphorylase
Autor: Bernd Nidetzky, Johanna Wiesbauer, Christiane Goedl, Lothar Brecker, Alexandra Schwarz
Publikováno v: Journal of Molecular Catalysis B: Enzymatic. 65:24-29
Stereoselective glycosylation of a phenolic hydroxyl is a key transformation in the (bio)synthesis of natural products. Biocatalytic transglycosylation usually provides the desired glycosidic product in exquisite anomeric purity. However, loss of sub
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::77f46d3bb417c7a0a3026835881c091c
https://doi.org/10.1016/j.molcatb.2009.12.007
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2
Sucrose phosphorylase: a powerful transglucosylation catalyst for synthesis of α-D-glucosides as industrial fine chemicals
Autor: Patricia Wildberger, Christiane Goedl, Bernd Nidetzky, Thornthan Sawangwan
Publikováno v: Biocatalysis and Biotransformation. 28:10-21
Sucrose phosphorylase is a bacterial transglucosidase that catalyzes conversion of sucrose and phosphate into α-D-glucose-1-phosphate and D-fructose. The enzyme utilizes a glycoside hydrolase-like double displacement mechanism that involves a cataly
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::53c5bab7b11e94dc0a7d4e6b1121314b
https://doi.org/10.3109/10242420903411595
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3
Glucosylglycerol and glucosylglycerate as enzyme stabilizers
Autor: Christiane Goedl, Thornthan Sawangwan, Bernd Nidetzky
Publikováno v: Biotechnology Journal. 5:187-191
Compatible solutes constitute a diverse class of low-molecular-mass organic molecules that are accumulated in high intracellular concentrations in response to the external stress of hyperosmolality or high temperature. Many of these compounds like al
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd824d82747c311f41770ee933d9a773
https://doi.org/10.1002/biot.200900197
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7
Studying non-covalent enzyme carbohydrate interactions by STD NMR
Autor: Bernd Nidetzky, Regina Kratzer, Christiane Goedl, Alexandra Schwarz, Catrin Tyl, Lothar Brecker
Publikováno v: Carbohydrate Research. 343:2153-2161
Saturation transfer difference NMR spectroscopy is used to study non-covalent interactions between four different glycostructure transforming enzymes and selected substrates and products. Resulting binding patterns represent a molecular basis of spec
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bb95d0ef12c5858b4ca937eb42c6ad4
https://doi.org/10.1016/j.carres.2007.12.023
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8
The phosphate site of trehalose phosphorylase from Schizophyllum commune probed by site-directed mutagenesis and chemical rescue studies
Autor: Christiane Goedl, Bernd Nidetzky
Publikováno v: FEBS Journal. 275:903-913
Schizophyllum communeα,α-trehalose phosphorylase utilizes a glycosyltransferase-like catalytic mechanism to convert its disaccharide substrate into α-d-glucose 1-phosphate and α-d-glucose. Recruitment of phosphate by the free enzyme induces α,α
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5f066600fff089850627bf75339f415a
https://doi.org/10.1111/j.1742-4658.2007.06254.x
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9
Trehalose phosphorylase from Pleurotus ostreatus: Characterization and stabilization by covalent modification, and application for the synthesis of α,α-trehalose
Autor: Bernd Nidetzky, Alphonse Minani, Christiane Goedl, Alexandra Schwarz
Publikováno v: Journal of Biotechnology. 129:140-150
Trehalose phosphorylase from the basidiomycete Pleurotus ostreatus (PoTPase) was isolated from fungal fruit bodies through approximately 500-fold purification with a yield of 44%. Combined analyses by SDS-PAGE and gelfiltration show that PoTPase is a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::006cff44062e3a5bb908ef69f15c5168
https://doi.org/10.1016/j.jbiotec.2006.11.022
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10
Structure–function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases
Autor: Bernd Nidetzky, Alexandra Schwarz, Christiane Goedl, Richard Griessler
Publikováno v: Biochemical Journal. 397:491-500
The cDNA encoding trehalose phosphorylase, a family GT-4 glycosyltransferase from the fungus Schizophyllum commune, was isolated and expressed in Escherichia coli to yield functional recombinant protein in its full length of 737 amino acids. Unlike t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::763b331c95b88b564c0dd9faeb1776bc
https://doi.org/10.1042/bj20060029
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