Modelling of Substrate Specificity of Various β-Glucosidases and UDP-Glucosyltransferases Exemplarily Done with Mycotoxin-β-D-Glucosides
A great amount of bioactive matter synthesised by microorganisms or plants can not be found naturally free in our environment. Diverse enzymes arrange for a glycosidic linkage, especially uridin-diphosphate-glycosyltransferases (UGTs). Likewise organisms own enzymes with differing substrate specificity that are able to free the bioactive substrates from their glycosidic linkage, so-called glycoside hydrolases (respectively glycosidases) of the GH1 family. It is of great interest to examine computationally the correlation between structure and substrate specificity of those groups of enzymes, which process different substrates.
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2012
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Olga Scharkoi, Susanne Esslinger, Roland Becker, Marcus Weber, Irene Nehls | Predicting sites of cytochrome P450-mediated hydroxylation applied to CYP3A4 and hexabromocyclododecane | Molecular Simulation, 2014 |
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2013 |
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Vedat Durmaz, Sebastian Schmidt, Peggy Sabri, Christian Piechotta, Marcus Weber | A hands-off linear interaction energy approach to binding mode and affinity estimation of estrogens | Journal of Chemical Information and Modeling, 53(10), pp. 2681-2688, 2013 |
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2012 |
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Vedat Durmaz, Marcus Weber, Roland Becker | How to Simulate Affinities for Host-Guest Systems Lacking Binding Mode Information: application to the liquid chromatographic separation of hexabromocyclododecane stereoisomers | Journal of Molecular Modeling, Vol.18, pp. 2399-2408, 2012 |
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