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 & Medical Chemistry 20(2): 622-627.

Journal Article | Published | English

No fulltext has been uploaded

Abstract
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.
Publishing Year
ISSN
PUB-ID

Cite this

Lenger J, Schröder M, Ennemann E, et al. Evaluation of sulfatase-directed quinone methide traps for proteomics. Bioorganic & Medical 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 & Medical 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 & Medical Chemistry 20, 622-627.
Lenger, J., et al., 2012. Evaluation of sulfatase-directed quinone methide traps for proteomics. Bioorganic & Medical Chemistry, 20(2), p 622-627.
J. Lenger, et al., “Evaluation of sulfatase-directed quinone methide traps for proteomics”, Bioorganic & Medical 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 & Medical 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 & Medical Chemistry 20.2 (2012): 622-627.
This data publication is cited in the following publications:
This publication cites the following data publications:

1 Citation in Europe PMC

Data provided by Europe PubMed Central.

19 References

Data provided by Europe PubMed Central.

Bioorthogonal organic chemistry in living cells: novel strategies for labeling biomolecules.
van Swieten PF, Leeuwenburgh MA, Kessler BM, Overkleeft HS., Org. Biomol. Chem. 3(1), 2005
PMID: 15602593

Hanson SR, Best MD, Wong C-H., 2004
Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship.
Sardiello M, Annunziata I, Roma G, Ballabio A., Hum. Mol. Genet. 14(21), 2005
PMID: 16174644

Bojarova P, Williams SJ., 2008
Sulfatases and human disease.
Diez-Roux G, Ballabio A., Annu Rev Genomics Hum Genet 6(), 2005
PMID: 16124866
A novel bacterial mucinase, glycosulfatase, is associated with bacterial vaginosis.
Roberton AM, Wiggins R, Horner PJ, Greenwood R, Crowley T, Fernandes A, Berry M, Corfield AP., J. Clin. Microbiol. 43(11), 2005
PMID: 16272477
Design and synthesis of class-selective activity probes for protein tyrosine phosphatases.
Lo LC, Pang TL, Kuo CH, Chiang YL, Wang HY, Lin JJ., J. Proteome Res. 1(1), 2002
PMID: 12643524
Activity-based protein profiling: new developments and directions in functional proteomics.
Uttamchandani M, Li J, Sun H, Yao SQ., Chembiochem 9(5), 2008
PMID: 18283695
Suicide inactivation of human prostatic acid phosphatase and a phosphotyrosine phosphatase.
Wang Q, Dechert U, Jirik F, Withers SG., Biochem. Biophys. Res. Commun. 200(1), 1994
PMID: 8166732
4-(Fluoromethyl)phenyl phosphate acts as a mechanism-based inhibitor of calcineurin.
Born TL, Myers JK, Widlanski TS, Rusnak F., J. Biol. Chem. 270(43), 1995
PMID: 7592741
The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase.
Szameit C, Miech C, Balleininger M, Schmidt B, von Figura K, Dierks T., J. Biol. Chem. 274(22), 1999
PMID: 10336424
Arylsulfatase G, a novel lysosomal sulfatase.
Frese MA, Schulz S, Dierks T., J. Biol. Chem. 283(17), 2008
PMID: 18283100
The non-catalytic N-terminal extension of formylglycine-generating enzyme is required for its biological activity and retention in the endoplasmic reticulum.
Mariappan M, Gande SL, Radhakrishnan K, Schmidt B, Dierks T, von Figura K., J. Biol. Chem. 283(17), 2008
PMID: 18305113
Steroid sulfatase. Biosynthesis and processing in normal and mutant fibroblasts.
Conary J, Nauerth A, Burns G, Hasilik A, von Figura K., Eur. J. Biochem. 158(1), 1986
PMID: 2942400
Structure-activity study on the quinone/quinone methide chemistry of flavonoids.
Awad HM, Boersma MG, Boeren S, van Bladeren PJ, Vervoort J, Rietjens IM., Chem. Res. Toxicol. 14(4), 2001
PMID: 11304128

Kalesh KA, Tan LP, Lu K, Gao L, Wang J, Yao SQ., 2010
Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine.
Miech C, Dierks T, Selmer T, von Figura K, Schmidt B., J. Biol. Chem. 273(9), 1998
PMID: 9478923

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 21570853
PubMed | Europe PMC

Search this title in

Google Scholar