Xia, Liqun ; Lin, Haili ; Staniek, Agata ; Panjikar, Santosh ; Ruppert, Martin ; Hilgers, Petra ; Williardt, Jörg ; Rajendran, Chitra ; Wang, Meitian ; Warzecha, Heribert ; Jäger, Volker ; Stöckigt, Joachim (2015)
Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours.
In: Journal of enzyme inhibition and medicinal chemistry, 30 (3)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Abstract Insight into the structure and inhibition mechanism of O-β-d-glucosidases by deoxa-pyranosylamine type inhibitors is provided by X-ray analysis of complexes between raucaffricine and strictosidine glucosidases and N-(cyclohexylmethyl)-, N-(cyclohexyl)- and N-(bromobenzyl)-β-d-gluco-1,5-deoxa-pyranosylamine. All inhibitors anchored exclusively in the catalytic active site by competition with appropriate enzyme substrates. Thus facilitated prospective elucidation of the binding networks with residues located at <3.9 Å distance will enable the development of potent inhibitors suitable for the production of valuable alkaloid glucosides, raucaffricine and strictosidine, by means of synthesis in Rauvolfia serpentina cell suspension cultures.
Typ des Eintrags: | Artikel |
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Erschienen: | 2015 |
Autor(en): | Xia, Liqun ; Lin, Haili ; Staniek, Agata ; Panjikar, Santosh ; Ruppert, Martin ; Hilgers, Petra ; Williardt, Jörg ; Rajendran, Chitra ; Wang, Meitian ; Warzecha, Heribert ; Jäger, Volker ; Stöckigt, Joachim |
Art des Eintrags: | Bibliographie |
Titel: | Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours. |
Sprache: | Englisch |
Publikationsjahr: | 2015 |
Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Journal of enzyme inhibition and medicinal chemistry |
Jahrgang/Volume einer Zeitschrift: | 30 |
(Heft-)Nummer: | 3 |
Kurzbeschreibung (Abstract): | Abstract Insight into the structure and inhibition mechanism of O-β-d-glucosidases by deoxa-pyranosylamine type inhibitors is provided by X-ray analysis of complexes between raucaffricine and strictosidine glucosidases and N-(cyclohexylmethyl)-, N-(cyclohexyl)- and N-(bromobenzyl)-β-d-gluco-1,5-deoxa-pyranosylamine. All inhibitors anchored exclusively in the catalytic active site by competition with appropriate enzyme substrates. Thus facilitated prospective elucidation of the binding networks with residues located at <3.9 Å distance will enable the development of potent inhibitors suitable for the production of valuable alkaloid glucosides, raucaffricine and strictosidine, by means of synthesis in Rauvolfia serpentina cell suspension cultures. |
Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Plant Biotechnology and Metabolic Engineering |
Hinterlegungsdatum: | 07 Jul 2015 08:20 |
Letzte Änderung: | 16 Sep 2015 11:36 |
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