Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine

Miech C, Dierks T, Selmer T, Figura von K, Schmidt B (1998)
JOURNAL OF BIOLOGICAL CHEMISTRY 273(9): 4835-4837.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Miech, C; Dierks, ThomasUniBi; Selmer, T; Figura von, K; Schmidt, B
Abstract / Bemerkung
Eukaryotic sulfatases share an unusual posttranslational protein modification, which converts a cysteine into alpha-formylglycine. The alpha-formylglycine is essential for the catalytic activity. Klebsiella pneumoniae expresses an inducible arylsulfatase for which the DNA predicts a serine at the position occupied by the alpha-formylglycine residue in eukaryotic sulfatases. Structural analysis showed that the majority of the arylsulfatase polypeptides from K. pneumoniae carries the alpha-formylglycine, whereas the remaining arylsulfatase polypeptides contain the predicted serine residue. This demonstrates the evolutionary conservation between prokaryotes and eukaryotes of this novel protein modification that so far has been found only in sulfatases. alpha-Formylglycine in Klebsiella is generated from a serine and not from a cysteine as in eukaryotes.
Erscheinungsjahr
1998
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
273
Ausgabe
9
Seite(n)
4835-4837
ISSN
0021-9258
Page URI
https://pub.uni-bielefeld.de/record/2350877

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Miech C, Dierks T, Selmer T, Figura von K, Schmidt B. Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. JOURNAL OF BIOLOGICAL CHEMISTRY. 1998;273(9):4835-4837.
Miech, C., Dierks, T., Selmer, T., Figura von, K., & Schmidt, B. (1998). Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. JOURNAL OF BIOLOGICAL CHEMISTRY, 273(9), 4835-4837. https://doi.org/10.1074/jbc.273.9.4835
Miech, C, Dierks, Thomas, Selmer, T, Figura von, K, and Schmidt, B. 1998. “Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine”. JOURNAL OF BIOLOGICAL CHEMISTRY 273 (9): 4835-4837.
Miech, C., Dierks, T., Selmer, T., Figura von, K., and Schmidt, B. (1998). Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. JOURNAL OF BIOLOGICAL CHEMISTRY 273, 4835-4837.
Miech, C., et al., 1998. Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. JOURNAL OF BIOLOGICAL CHEMISTRY, 273(9), p 4835-4837.
C. Miech, et al., “Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 273, 1998, pp. 4835-4837.
Miech, C., Dierks, T., Selmer, T., Figura von, K., Schmidt, B.: Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. JOURNAL OF BIOLOGICAL CHEMISTRY. 273, 4835-4837 (1998).
Miech, C, Dierks, Thomas, Selmer, T, Figura von, K, and Schmidt, B. “Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine”. JOURNAL OF BIOLOGICAL CHEMISTRY 273.9 (1998): 4835-4837.

41 Zitationen in Europe PMC

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Structural distortions due to missense mutations in human formylglycine-generating enzyme leading to multiple sulfatase deficiency.
Meshach Paul D, Chadah T, Senthilkumar B, Sethumadhavan R, Rajasekaran R., J Biomol Struct Dyn 36(13), 2018
PMID: 29048999
A natural variant of arylsulfatase from Kluyveromyces lactis shows no formylglycine modification and has no enzyme activity.
Stressler T, Reichenberger K, Glück C, Leptihn S, Pfannstiel J, Swietalski P, Kuhn A, Seitl I, Fischer L., Appl Microbiol Biotechnol 102(6), 2018
PMID: 29450617
Assimilation of alternative sulfur sources in fungi.
Linder T., World J Microbiol Biotechnol 34(4), 2018
PMID: 29550883
Two-fold Bioorthogonal Derivatization by Different Formylglycine-Generating Enzymes.
Krüger T, Weiland S, Falck G, Gerlach M, Boschanski M, Alam S, Müller KM, Dierks T, Sewald N., Angew Chem Int Ed Engl 57(24), 2018
PMID: 29579347
Characterization of an arylsulfatase from a mutant library of Pseudoalteromonas carrageenovora arylsulfatase.
Zhu Y, Liu H, Qiao C, Li L, Jiang Z, Xiao A, Ni H., Int J Biol Macromol 96(), 2017
PMID: 27940339
Homologous expression and biochemical characterization of the arylsulfatase from Kluyveromyces lactis and its relevance in milk processing.
Stressler T, Leisibach D, Lutz-Wahl S, Kuhn A, Fischer L., Appl Microbiol Biotechnol 100(12), 2016
PMID: 26875879
Enzymatic desulfation of the red seaweeds agar by Marinomonas arylsulfatase.
Wang X, Duan D, Fu X., Int J Biol Macromol 93(pt a), 2016
PMID: 27521846
Detection, production, and application of microbial arylsulfatases.
Stressler T, Seitl I, Kuhn A, Fischer L., Appl Microbiol Biotechnol 100(21), 2016
PMID: 27654655
Matching the Diversity of Sulfated Biomolecules: Creation of a Classification Database for Sulfatases Reflecting Their Substrate Specificity.
Barbeyron T, Brillet-Guéguen L, Carré W, Carrière C, Caron C, Czjzek M, Hoebeke M, Michel G., PLoS One 11(10), 2016
PMID: 27749924
Glycosulfatase-Encoding Gene Cluster in Bifidobacterium breve UCC2003.
Egan M, Jiang H, O'Connell Motherway M, Oscarson S, van Sinderen D., Appl Environ Microbiol 82(22), 2016
PMID: 27590817
Mucopolysaccharidosis enzyme production by bone marrow and dental pulp derived human mesenchymal stem cells.
Jackson M, Derrick Roberts A, Martin E, Rout-Pitt N, Gronthos S, Byers S., Mol Genet Metab 114(4), 2015
PMID: 25748347
Deep Genotyping of the IDS Gene in Colombian Patients with Hunter Syndrome.
Galvis J, González J, Uribe A, Velasco H., JIMD Rep 19(), 2015
PMID: 25681085
Pseudomonas aeruginosa arylsulfatase: a purified enzyme for the mild hydrolysis of steroid sulfates.
Stevenson BJ, Waller CC, Ma P, Li K, Cawley AT, Ollis DL, McLeod MD., Drug Test Anal 7(10), 2015
PMID: 25739756
Low-scale expression and purification of an active putative iduronate 2-sulfate sulfatase-Like enzyme from Escherichia coli K12.
Morales-Álvarez ED, Rivera-Hoyos CM, Baena-Moncada AM, Landázuri P, Poutou-Piñales RA, Sáenz-Suárez H, Barrera LA, Echeverri-Peña OY., J Microbiol 51(2), 2013
PMID: 23625223
Evaluation of sulfatase-directed quinone methide traps for proteomics.
Lenger J, Schröder M, Ennemann EC, Müller B, Wong CH, Noll T, Dierks T, Hanson SR, Sewald N., Bioorg Med Chem 20(2), 2012
PMID: 21570853
Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals.
Gande SL, Mariappan M, Schmidt B, Pringle TH, von Figura K, Dierks T., FEBS J 275(6), 2008
PMID: 18266766
In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters.
Grove TL, Lee KH, St Clair J, Krebs C, Booker SJ., Biochemistry 47(28), 2008
PMID: 18558715
Purification and characterization of the recombinant arylsulfatase cloned from Pseudoalteromonas carrageenovora.
Kim DE, Kim KH, Bae YJ, Lee JH, Jang YH, Nam SW., Protein Expr Purif 39(1), 2005
PMID: 15596366
Sulfatases and human disease.
Diez-Roux G, Ballabio A., Annu Rev Genomics Hum Genet 6(), 2005
PMID: 16124866
Analysis of normal and mutant iduronate-2-sulphatase conformation.
Parkinson-Lawrence E, Turner C, Hopwood J, Brooks D., Biochem J 386(pt 2), 2005
PMID: 15500445
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
Dierks T, Dickmanns A, Preusser-Kunze A, Schmidt B, Mariappan M, von Figura K, Ficner R, Rudolph MG., Cell 121(4), 2005
PMID: 15907468
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
Highly enantioselective sec-alkyl sulfatase activity of the marine planctomycete Rhodopirellula baltica shows retention of configuration.
Wallner SR, Bauer M, Würdemann C, Wecker P, Glöckner FO, Faber K., Angew Chem Int Ed Engl 44(39), 2005
PMID: 16161167
Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility.
Hanson SR, Best MD, Wong CH., Angew Chem Int Ed Engl 43(43), 2004
PMID: 15493058
Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.
Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K., Cell 113(4), 2003
PMID: 12757705
1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family.
Boltes I, Czapinska H, Kahnert A, von Bülow R, Dierks T, Schmidt B, von Figura K, Kertesz MA, Usón I., Structure 9(6), 2001
PMID: 11435113
Novel cofactors via post-translational modifications of enzyme active sites.
Okeley NM, van der Donk WA., Chem Biol 7(7), 2000
PMID: 10903941
Escherichia coli K1 aslA contributes to invasion of brain microvascular endothelial cells in vitro and in vivo.
Hoffman JA, Badger JL, Zhang Y, Huang SH, Kim KS., Infect Immun 68(9), 2000
PMID: 10948126
Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases.
Dierks T, Lecca MR, Schlotterhose P, Schmidt B, von Figura K., EMBO J 18(8), 1999
PMID: 10205163
A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease.
von Figura K, Schmidt B, Selmer T, Dierks T., Bioessays 20(6), 1998
PMID: 9699462
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