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, Figura von K, Ficner R, Rudolph MG (2005)
CELL 121(4): 541-552.

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Abstract
Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate.
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Dierks T, Dickmanns A, Preusser-Kunze A, et al. Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL. 2005;121(4):541-552.
Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., Figura von, K., Ficner, R., et al. (2005). Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL, 121(4), 541-552. doi:10.1016/j.cell.2005.03.001
Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., Figura von, K., Ficner, R., and Rudolph, M. G. (2005). Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL 121, 541-552.
Dierks, T., et al., 2005. Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL, 121(4), p 541-552.
T. Dierks, et al., “Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme”, CELL, vol. 121, 2005, pp. 541-552.
Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., Figura von, K., Ficner, R., Rudolph, M.G.: Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. CELL. 121, 541-552 (2005).
Dierks, Thomas, Dickmanns, A, Preusser-Kunze, A, Schmidt, B, Mariappan, M, Figura von, K, Ficner, R, and Rudolph, MG. “Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme”. CELL 121.4 (2005): 541-552.
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Muhlberg M, Hoesl MG, Kuehne C, Dernedde J, Budisa N, Hackenberger CP., Beilstein J Org Chem 11(), 2015
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Effects of glycosylation and pH conditions in the dynamics of human arylsulfatase A.
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Effects of open versus laparoscopic nephrectomy techniques on oxidative stress markers in patients with renal cell carcinoma.
Mila-Kierzenkowska C, Wozniak A, Drewa T, Wozniak B, Szpinda M, Krzyzynska-Malinowska E, Rajewski P., Oxid Med Cell Longev 2013(), 2013
PMID: 23533691
HpSumf1 is involved in the activation of sulfatases responsible for regulation of skeletogenesis during sea urchin development.
Sakuma T, Ohnishi K, Fujita K, Ochiai H, Sakamoto N, Yamamoto T., Dev. Genes Evol. 221(3), 2011
PMID: 21706447
Multiple sulfatase deficiency: clinical report and description of two novel mutations in a Brazilian patient.
Artigalas OA, da Silva LR, Burin M, Pastores GM, Zeng B, Macedo N, Schwartz IV., Metab Brain Dis 24(3), 2009
PMID: 19697114
Biomacromolecular interactions, assemblies and machines: a structural view.
Heinz DW, Weiss MS, Wendt KU., Chembiochem 7(1), 2006
PMID: 16317791

54 References

Data provided by Europe PubMed Central.

Biochemical basis of oxidative protein folding in the endoplasmic reticulum.
Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS., Science 290(5496), 2000
PMID: 11090354
Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes.
Vranka JA, Sakai LY, Bachinger HP., J. Biol. Chem. 279(22), 2004
PMID: 15044469

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