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.

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.
Erscheinungsjahr
2005
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
280
Ausgabe
15
Seite(n)
14900-14910
ISSN
0021-9258
eISSN
1083-351X
Page URI
https://pub.uni-bielefeld.de/record/1603995

Zitieren

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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