Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours

Liqun Xia; Haili Lin; Agata Staniek; Santosh Panjikar; Martin Ruppert; Petra Hilgers; Jorg Williardt; Chitra Rajendran; Meitian Wang; Heribert Warzecha; Volker Jager; Joachim Stockigt

doi:10.3109/14756366.2014.949252

Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours

Liqun Xia, Haili Lin, Agata Staniek, Santosh Panjikar, Martin Ruppert, Petra Hilgers, Jorg Williardt, Chitra Rajendran, Meitian Wang, Heribert Warzecha, Volker Jager, Joachim Stockigt

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

1 Citation (Scopus)

Abstract

Abstract Insight into the structure and inhibition mechanism of O-beta-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)-beta-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

Original language	English
Pages (from-to)	472 - 478
Number of pages	7
Journal	Journal of Enzyme Inhibition and Medicinal Chemistry
Volume	30
Issue number	3
DOIs	https://doi.org/10.3109/14756366.2014.949252
Publication status	Published - 2015

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Xia, L., Lin, H., Staniek, A., Panjikar, S., Ruppert, M., Hilgers, P., Williardt, J., Rajendran, C., Wang, M., Warzecha, H., Jager, V., & Stockigt, J. (2015). Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours. Journal of Enzyme Inhibition and Medicinal Chemistry, 30(3), 472 - 478. https://doi.org/10.3109/14756366.2014.949252

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title = "Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours",

abstract = "Abstract Insight into the structure and inhibition mechanism of O-beta-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)-beta-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",

author = "Liqun Xia and Haili Lin and Agata Staniek and Santosh Panjikar and Martin Ruppert and Petra Hilgers and Jorg Williardt and Chitra Rajendran and Meitian Wang and Heribert Warzecha and Volker Jager and Joachim Stockigt",

year = "2015",

doi = "10.3109/14756366.2014.949252",

language = "English",

volume = "30",

pages = "472 -- 478",

journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",

issn = "1475-6366",

publisher = "Taylor & Francis",

number = "3",

}

Xia, L, Lin, H, Staniek, A, Panjikar, S, Ruppert, M, Hilgers, P, Williardt, J, Rajendran, C, Wang, M, Warzecha, H, Jager, V & Stockigt, J 2015, 'Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours', Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 30, no. 3, pp. 472 - 478. https://doi.org/10.3109/14756366.2014.949252

Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours. / Xia, Liqun; Lin, Haili; Staniek, Agata et al.
In: Journal of Enzyme Inhibition and Medicinal Chemistry, Vol. 30, No. 3, 2015, p. 472 - 478.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours

AU - Xia, Liqun

AU - Lin, Haili

AU - Staniek, Agata

AU - Panjikar, Santosh

AU - Ruppert, Martin

AU - Hilgers, Petra

AU - Williardt, Jorg

AU - Rajendran, Chitra

AU - Wang, Meitian

AU - Warzecha, Heribert

AU - Jager, Volker

AU - Stockigt, Joachim

PY - 2015

Y1 - 2015

N2 - Abstract Insight into the structure and inhibition mechanism of O-beta-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)-beta-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

AB - Abstract Insight into the structure and inhibition mechanism of O-beta-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)-beta-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

UR - http://informahealthcare.com/doi/pdf/10.3109/14756366.2014.949252

U2 - 10.3109/14756366.2014.949252

DO - 10.3109/14756366.2014.949252

M3 - Article

SN - 1475-6366

VL - 30

SP - 472

EP - 478

JO - Journal of Enzyme Inhibition and Medicinal Chemistry

JF - Journal of Enzyme Inhibition and Medicinal Chemistry

IS - 3

ER -

Ligand structures of synthetic deoxa-pyranosylamines with raucaffricine and strictosidine glucosidases provide structural insights into their binding and inhibitory behaviours

Abstract

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