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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

FGly     2-formamidoethanoic acid

Synonyms: Formylglycin, Formylglycine, ACMC-1CB19, AG-B-76023, CHEBI:16180, ...
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Disease relevance of Formylglycine


High impact information on Formylglycine


Chemical compound and disease context of Formylglycine


Biological context of Formylglycine


Anatomical context of Formylglycine


Associations of Formylglycine with other chemical compounds

  • The formylglycine acts as an aldehyde hydrate with two geminal hydroxyls being involved in catalysis of sulfate ester cleavage [12].
  • We postulate that this N-terminal region of FGE mediates the interaction with an ER component to be identified and that this interaction is required for both the generation of FGly residues in nascent sulfatase polypeptides and for retention of FGE in the ER [13].

Gene context of Formylglycine


Analytical, diagnostic and therapeutic context of Formylglycine


  1. The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase. Szameit, C., Miech, C., Balleininger, M., Schmidt, B., von Figura, K., Dierks, T. J. Biol. Chem. (1999) [Pubmed]
  2. Coexpression of formylglycine-generating enzyme is essential for synthesis and secretion of functional arylsulfatase A in a mouse model of metachromatic leukodystrophy. Takakusaki, Y., Hisayasu, S., Hirai, Y., Shimada, T. Hum. Gene Ther. (2005) [Pubmed]
  3. 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, M.G. Cell (2005) [Pubmed]
  4. Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Dierks, T., Schmidt, B., von Figura, K. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. Expression, localization, structural, and functional characterization of pFGE, the paralog of the Calpha-formylglycine-generating enzyme. Mariappan, M., Preusser-Kunze, A., Balleininger, M., Eiselt, N., Schmidt, B., Gande, S.L., Wenzel, D., Dierks, T., von Figura, K. J. Biol. Chem. (2005) [Pubmed]
  6. Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum. Fey, J., Balleininger, M., Borissenko, L.V., Schmidt, B., von Figura, K., Dierks, T. J. Biol. Chem. (2001) [Pubmed]
  7. Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. Miech, C., Dierks, T., Selmer, T., von Figura, K., Schmidt, B. J. Biol. Chem. (1998) [Pubmed]
  8. Sulfatases, trapping of the sulfated enzyme intermediate by substituting the active site formylglycine. Recksiek, M., Selmer, T., Dierks, T., Schmidt, B., von Figura, K. J. Biol. Chem. (1998) [Pubmed]
  9. Residues critical for formylglycine formation and/or catalytic activity of arylsulfatase A. Knaust, A., Schmidt, B., Dierks, T., von Bülow, R., von Figura, K. Biochemistry (1998) [Pubmed]
  10. Three-dimensional structures of sulfatases. Ghosh, D. Meth. Enzymol. (2005) [Pubmed]
  11. Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. Dierks, T., Lecca, M.R., Schmidt, B., von Figura, K. FEBS Lett. (1998) [Pubmed]
  12. Amino acid residues forming the active site of arylsulfatase A. Role in catalytic activity and substrate binding. Waldow, A., Schmidt, B., Dierks, T., von Bülow, R., von Figura, K. J. Biol. Chem. (1999) [Pubmed]
  13. The non-catalytic N-terminal extension of formylglycine-generating enzyme is required for its biological activity and retention in the endoplasmic reticulum. Mariappan, M., Gande, S.L., Radhakrishnan, K., Schmidt, B., Dierks, T., von Figura, K. J. Biol. Chem. (2008) [Pubmed]
  14. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. Dierks, T., Miech, C., Hummerjohann, J., Schmidt, B., Kertesz, M.A., von Figura, K. J. Biol. Chem. (1998) [Pubmed]
  15. The heparin/heparan sulfate 2-O-sulfatase from Flavobacterium heparinum. A structural and biochemical study of the enzyme active site and saccharide substrate specificity. Raman, R., Myette, J.R., Shriver, Z., Pojasek, K., Venkataraman, G., Sasisekharan, R. J. Biol. Chem. (2003) [Pubmed]
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