Evaluation of sulfatase-directed quinone methide traps for proteomics
Lenger J, Schröder M, Ennemann E, Müller B, Wong C-H, Noll T, Dierks T, Hanson SR, Sewald N (2012)
Bioorganic & Medicinal Chemistry 20(2): 622-627.
Zeitschriftenaufsatz
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Autor*in
Lenger, JaninaUniBi;
Schröder, MariusUniBi;
Ennemann, EvaUniBi;
Müller, BenjaminUniBi;
Wong, C.-H.;
Noll, ThomasUniBi ;
Dierks, ThomasUniBi;
Hanson, Sarah R.;
Sewald, NorbertUniBi
Einrichtung
Fakultät für Chemie > Organische Chemie III
Centrum für Biotechnologie > Graduate Center > Graduate Cluster Industrial Biotechnology
Centrum für Biotechnologie > Arbeitsgruppe T. Noll
Centrum für Biotechnologie > Arbeitsgruppe T. Dierks
Technische Fakultät > AG Zellkulturtechnik
Centrum für Biotechnologie > Arbeitsgruppe N. Sewald
Centrum für Biotechnologie > Institut für Biochemie und Biotechnik
Fakultät für Chemie > Biochemie I
Centrum für Biotechnologie > Graduate Center > Graduate Cluster Industrial Biotechnology
Centrum für Biotechnologie > Arbeitsgruppe T. Noll
Centrum für Biotechnologie > Arbeitsgruppe T. Dierks
Technische Fakultät > AG Zellkulturtechnik
Centrum für Biotechnologie > Arbeitsgruppe N. Sewald
Centrum für Biotechnologie > Institut für Biochemie und Biotechnik
Fakultät für Chemie > Biochemie I
Abstract / Bemerkung
Sulfatases hydrolytically cleave sulfate esters through a unique catalytic aldehyde, which is introduced by a posttranslational oxidation. To profile active sulfatases in health and disease, activity-based proteomic tools are needed. Herein, quinone methide (QM) traps directed against sulfatases are evaluated as activity-based proteomic probes (ABPPs). Starting from a p-fluoromethylphenyl sulfate scaffold, enzymatically generated QM-traps can inactivate bacterial aryl sulfatases from Pseudomonas aeruginosa and Klebsiella pneumoniae, and human steroid sulfatase. However, multiple enzyme-generated QMs form, diffuse, and non-specifically label purified enzyme. In complex proteomes, QM labeling is sulfatase-dependent but also non-specific. Thus, fluoromethylphenyl sulfates are poor ABPPs for sulfatases.
Erscheinungsjahr
2012
Zeitschriftentitel
Bioorganic & Medicinal Chemistry
Band
20
Ausgabe
2
Seite(n)
622-627
ISSN
0968-0896
Page URI
https://pub.uni-bielefeld.de/record/2351519
Zitieren
Lenger J, Schröder M, Ennemann E, et al. Evaluation of sulfatase-directed quinone methide traps for proteomics. Bioorganic & Medicinal Chemistry. 2012;20(2):622-627.
Lenger, J., Schröder, M., Ennemann, E., Müller, B., Wong, C. - H., Noll, T., Dierks, T., et al. (2012). Evaluation of sulfatase-directed quinone methide traps for proteomics. Bioorganic & Medicinal Chemistry, 20(2), 622-627. https://doi.org/10.1016/j.bmc.2011.04.044
Lenger, Janina, Schröder, Marius, Ennemann, Eva, Müller, Benjamin, Wong, C.-H., Noll, Thomas, Dierks, Thomas, Hanson, Sarah R., and Sewald, Norbert. 2012. “Evaluation of sulfatase-directed quinone methide traps for proteomics”. Bioorganic & Medicinal Chemistry 20 (2): 622-627.
Lenger, J., Schröder, M., Ennemann, E., Müller, B., Wong, C. - H., Noll, T., Dierks, T., Hanson, S. R., and Sewald, N. (2012). Evaluation of sulfatase-directed quinone methide traps for proteomics. Bioorganic & Medicinal Chemistry 20, 622-627.
Lenger, J., et al., 2012. Evaluation of sulfatase-directed quinone methide traps for proteomics. Bioorganic & Medicinal Chemistry, 20(2), p 622-627.
J. Lenger, et al., “Evaluation of sulfatase-directed quinone methide traps for proteomics”, Bioorganic & Medicinal Chemistry, vol. 20, 2012, pp. 622-627.
Lenger, J., Schröder, M., Ennemann, E., Müller, B., Wong, C.-H., Noll, T., Dierks, T., Hanson, S.R., Sewald, N.: Evaluation of sulfatase-directed quinone methide traps for proteomics. Bioorganic & Medicinal Chemistry. 20, 622-627 (2012).
Lenger, Janina, Schröder, Marius, Ennemann, Eva, Müller, Benjamin, Wong, C.-H., Noll, Thomas, Dierks, Thomas, Hanson, Sarah R., and Sewald, Norbert. “Evaluation of sulfatase-directed quinone methide traps for proteomics”. Bioorganic & Medicinal Chemistry 20.2 (2012): 622-627.
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