Molecular characterization of the human C alpha-formylglycine-generating enzyme

Preusser-Kunze A, Mariappan M, Schmidt B, Gande SL, Mutenda K, Wenzel K, von Figura K, Dierks T (2005)
JOURNAL OF BIOLOGICAL CHEMISTRY 280(15): 14900-14910.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
alpha-formylglycine (FGly) is the catalytic residue in the active site of sulfatases. In eukaryotes, it is generated in the endoplasmic reticulum by post-translational modification of a conserved cysteine residue. The FGly-generating enzyme (FGE), performing this modification, is an endoplasmic reticulum-resident enzyme that upon overexpression is secreted. Recombinant FGE was purified from cells and secretions to homogeneity. Intracellular FGE contains a high mannose type N-glycan, which is processed to the complex type in secreted FGE. Secreted FGE shows partial N-terminal trimming up to residue 73 without loosing catalytic activity. FGE is a calcium-binding protein containing an N-terminal (residues 86 168) and a C-terminal (residues 178-374) protease-resistant domain. The latter is stabilized by three disulfide bridges arranged in a clamp-like manner, which links the third to the eighth, the fourth to the seventh, and the fifth to the sixth cysteine residue. The innermost cysteine pair is partially reduced. The first two cysteine residues are located in the sequence preceding the N-terminal protease-resistant domain. They can form intramolecular or intermolecular disulfide bonds, the latter stabilizing homodimers. The C-terminal domain comprises the substrate binding site, as evidenced by yeast two-hybrid interaction assays and photocross-linking of a substrate peptide to proline 182. Peptides derived from all known human sulfatases served as substrates for purified FGE indicating that FGE is sufficient to modify all sulfatases of the same species.
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Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
280
Zeitschriftennummer
15
Seite
14900-14910
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eISSN
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Preusser-Kunze A, Mariappan M, Schmidt B, et al. Molecular characterization of the human C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY. 2005;280(15):14900-14910.
Preusser-Kunze, A., Mariappan, M., Schmidt, B., Gande, S. L., Mutenda, K., Wenzel, K., von Figura, K., et al. (2005). Molecular characterization of the human C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY, 280(15), 14900-14910. doi:10.1074/jbc.M413383200
Preusser-Kunze, A., Mariappan, M., Schmidt, B., Gande, S. L., Mutenda, K., Wenzel, K., von Figura, K., and Dierks, T. (2005). Molecular characterization of the human C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY 280, 14900-14910.
Preusser-Kunze, A., et al., 2005. Molecular characterization of the human C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY, 280(15), p 14900-14910.
A. Preusser-Kunze, et al., “Molecular characterization of the human C alpha-formylglycine-generating enzyme”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 280, 2005, pp. 14900-14910.
Preusser-Kunze, A., Mariappan, M., Schmidt, B., Gande, S.L., Mutenda, K., Wenzel, K., von Figura, K., Dierks, T.: Molecular characterization of the human C alpha-formylglycine-generating enzyme. JOURNAL OF BIOLOGICAL CHEMISTRY. 280, 14900-14910 (2005).
Preusser-Kunze, A, Mariappan, M, Schmidt, B, Gande, SL, Mutenda, K, Wenzel, K, von Figura, K, and Dierks, Thomas. “Molecular characterization of the human C alpha-formylglycine-generating enzyme”. JOURNAL OF BIOLOGICAL CHEMISTRY 280.15 (2005): 14900-14910.

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PMID: 28464818
Insights into Hunter syndrome from the structure of iduronate-2-sulfatase.
Demydchuk M, Hill CH, Zhou A, Bunkóczi G, Stein PE, Marchesan D, Deane JE, Read RJ., Nat Commun 8(), 2017
PMID: 28593992
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 (), 2017
PMID: 29048999
Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum.
Zito E, Buono M, Pepe S, Settembre C, Annunziata I, Surace EM, Dierks T, Monti M, Cozzolino M, Pucci P, Ballabio A, Cosma MP., EMBO J 35(23), 2016
PMID: 27908960
Reconstitution of Formylglycine-generating Enzyme with Copper(II) for Aldehyde Tag Conversion.
Holder PG, Jones LC, Drake PM, Barfield RM, Bañas S, de Hart GW, Baker J, Rabuka D., J Biol Chem 290(25), 2015
PMID: 25931126
Investigations into the Biosynthesis, Regulation, and Self-Resistance of Toxoflavin in Pseudomonas protegens Pf-5.
Philmus B, Shaffer BT, Kidarsa TA, Yan Q, Raaijmakers JM, Begley TP, Loper JE., Chembiochem 16(12), 2015
PMID: 26077901
Eukaryotic formylglycine-generating enzyme catalyses a monooxygenase type of reaction.
Peng J, Alam S, Radhakrishnan K, Mariappan M, Rudolph MG, May C, Dierks T, von Figura K, Schmidt B., FEBS J 282(17), 2015
PMID: 26077311
The Regulation of Steroid Action by Sulfation and Desulfation.
Mueller JW, Gilligan LC, Idkowiak J, Arlt W, Foster PA., Endocr Rev 36(5), 2015
PMID: 26213785
In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I).
Knop M, Engi P, Lemnaru R, Seebeck FP., Chembiochem 16(15), 2015
PMID: 26403223
Downregulation of SUMF2 gene in ovalbumin-induced rat model of allergic inflammation.
Fang C, Li X, Liang H, Xue L, Liu L, Yang C, Gao G, Jiang X., Int J Clin Exp Pathol 8(10), 2015
PMID: 26722390
Chemoenzymatic Fc glycosylation via engineered aldehyde tags.
Smith EL, Giddens JP, Iavarone AT, Godula K, Wang LX, Bertozzi CR., Bioconjug Chem 25(4), 2014
PMID: 24702330
Proprotein convertases process and thereby inactivate formylglycine-generating enzyme.
Ennemann EC, Radhakrishnan K, Mariappan M, Wachs M, Pringle TH, Schmidt B, Dierks T., J Biol Chem 288(8), 2013
PMID: 23288839
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Schlotawa L, Radhakrishnan K, Baumgartner M, Schmid R, Schmidt B, Dierks T, Gärtner J., Eur J Hum Genet 21(9), 2013
PMID: 23321616
Arylsulfatase K, a novel lysosomal sulfatase.
Wiegmann EM, Westendorf E, Kalus I, Pringle TH, Lübke T, Dierks T., J Biol Chem 288(42), 2013
PMID: 23986440
SUMF1 mutations affecting stability and activity of formylglycine generating enzyme predict clinical outcome in multiple sulfatase deficiency.
Schlotawa L, Ennemann EC, Radhakrishnan K, Schmidt B, Chakrapani A, Christen HJ, Moser H, Steinmann B, Dierks T, Gärtner J., Eur J Hum Genet 19(3), 2011
PMID: 21224894
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
Cofactor-independent oxidases and oxygenases.
Fetzner S, Steiner RA., Appl Microbiol Biotechnol 86(3), 2010
PMID: 20157809
Dominant negative mutations affect oligomerization of human pyruvate kinase M2 isozyme and promote cellular growth and polyploidy.
Gupta V, Kalaiarasan P, Faheem M, Singh N, Iqbal MA, Bamezai RN., J Biol Chem 285(22), 2010
PMID: 20304929
Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1.
Kollmann K, Damme M, Deuschl F, Kahle J, D'Hooge R, Lüllmann-Rauch R, Lübke T., FEBS J 276(5), 2009
PMID: 19187242
Characterization of the human sulfatase Sulf1 and its high affinity heparin/heparan sulfate interaction domain.
Frese MA, Milz F, Dick M, Lamanna WC, Dierks T., J Biol Chem 284(41), 2009
PMID: 19666466
Multiple sulfatase deficiency: clinical report and description of two novel mutations in a Brazilian patient.
Artigalás OA, da Silva LR, Burin M, Pastores GM, Zeng B, Macedo N, Schwartz IV., Metab Brain Dis 24(3), 2009
PMID: 19697114
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
Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44.
Fraldi A, Zito E, Annunziata F, Lombardi A, Cozzolino M, Monti M, Spampanato C, Ballabio A, Pucci P, Sitia R, Cosma MP., Hum Mol Genet 17(17), 2008
PMID: 18508857
Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum.
Zito E, Buono M, Pepe S, Settembre C, Annunziata I, Surace EM, Dierks T, Monti M, Cozzolino M, Pucci P, Ballabio A, Cosma MP., EMBO J 26(10), 2007
PMID: 17446859
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
PMID: 16368756
Sulfatases and human disease.
Diez-Roux G, Ballabio A., Annu Rev Genomics Hum Genet 6(), 2005
PMID: 16124866
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
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PMID: 15907468

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