Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum

Dierks T, Lecca MR, Schmidt B, Figura von K (1998)
FEBS LETTERS 423(1): 61-65.

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Sulfatases undergo an unusual protein modification leading to conversion of a specific cysteine residue into alpha-formylglycine. This conversion is essential for catalytic activity. In arylsulfatase A the alpha-formylglycine is generated inside the endoplasmic reticulum at a]ate stage of protein translocation. Using in vitro translation in the presence of transport-competent microsomes we found that arylsulfatase B is also modified in a similar way by the formylglycine-generating machinery. Modification depended on protein transport and on the correct position of the relevant cysteine. Arylsulfatase A and B did not compete for modification, as became apparent in co-expression experiments. This could argue for an association of the modification machinery with the protein translocation apparatus. (C) 1998 Federation of European Biochemical Societies.
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Dierks T, Lecca MR, Schmidt B, Figura von K. Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS LETTERS. 1998;423(1):61-65.
Dierks, T., Lecca, M. R., Schmidt, B., & Figura von, K. (1998). Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS LETTERS, 423(1), 61-65.
Dierks, T., Lecca, M. R., Schmidt, B., and Figura von, K. (1998). Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS LETTERS 423, 61-65.
Dierks, T., et al., 1998. Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS LETTERS, 423(1), p 61-65.
T. Dierks, et al., “Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum”, FEBS LETTERS, vol. 423, 1998, pp. 61-65.
Dierks, T., Lecca, M.R., Schmidt, B., Figura von, K.: Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS LETTERS. 423, 61-65 (1998).
Dierks, Thomas, Lecca, MR, Schmidt, B, and Figura von, K. “Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum”. FEBS LETTERS 423.1 (1998): 61-65.
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14 Citations in Europe PMC

Data provided by Europe PubMed Central.

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Low-scale expression and purification of an active putative iduronate 2-sulfate sulfatase-Like enzyme from Escherichia coli K12.
Morales-Alvarez ED, Rivera-Hoyos CM, Baena-Moncada AM, Landazuri P, Poutou-Pinales RA, Saenz-Suarez H, Barrera LA, Echeverri-Pena OY., J. Microbiol. 51(2), 2013
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Arylsulfatase B improves locomotor function after mouse spinal cord injury.
Yoo M, Khaled M, Gibbs KM, Kim J, Kowalewski B, Dierks T, Schachner M., PLoS ONE 8(3), 2013
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A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.
Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG., Proc. Natl. Acad. Sci. U.S.A. 103(1), 2006
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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
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Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility.
Hanson SR, Best MD, Wong CH., Angew. Chem. Int. Ed. Engl. 43(43), 2004
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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
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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
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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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