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.

Download
No fulltext has been uploaded. References only!
Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ; ;
Abstract
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.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

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.
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.
This data publication is cited in the following publications:
This publication cites the following data publications:

32 Citations in Europe PMC

Data provided by Europe PubMed Central.

In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I).
Knop M, Engi P, Lemnaru R, Seebeck FP., Chembiochem 16(15), 2015
PMID: 26403223
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
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

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 15657036
PubMed | Europe PMC

Search this title in

Google Scholar