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Production and Therapeutic use of active Formylglycine-Generating-Enzyme (FGE)

Organization name

MBM ScienceBridge GmbH


In a collaboration scientists from the University of Göttingen and of the University of Bielefeld developed a procedure for the production of recombinant isolated active eukaryotic full lenght C-alpha Formylglycine-Generating Enzyme (FGE) in selected eukaryotic cells for biotechnological and therapeutic uses.


Sulfatases are essential enzymes for humans, with Formylglycine (Fgly) as the key catalytic residue in the active site. Fgly is generated post-translationally in higher eukaryotes from a cysteine precursor by the Fgly-generating enzyme (FGE). FGE is cleaved and truncated by furin, PACE4 and PC5a. Inactivity of FGE reduces the activity of sulfatases, all of which results in in Multiple Sulfatase Deficiency (MSD Austin-Syndrome). Estimated prevalence of MSD is 1:1.4 million births. Deficiency of individual sulfatases can result in different clinical diseases, e.g. mucopolysaccharidosis II, IIA, IID, IVA and VI, metachromatic leukodystrophy, X-linked ichthyosis and the X-linked recessive form of chondrodysplasia punctata. These diseases also belong to the Lysosomal Storage Diseases (LSD).

Current challenges and needs include: Current production of FGE has the problem of post-translational cleavage of the N-terminal region.This N-terminal truncated (delta 72) eukaryotic enzyme is non-functional in vivo and requires the presence of strong reducing agents such as DTT to be active in vitro.

There is a need for the provision & production of active full length (fl) eukaryotic FGE capable of generating formylglycine. The N-terminal extension of human FGE is required for activation of sulfatases in cultured cells, and it confers efficient retention of FGE in the ER.

Our Solution

The scientists developed a new expression/production system for an efficient production of non truncated active full length FGE and its variants. The process is performed in a selected eukaryotic cells achieving high amounts of product. An optimized designed mutation in e.g. Arg69 and/or Arg72 has been included to avoid N-truncation. No further FGE degradation is observed, e.g. in the ER.


  • Catalytically active full length eukaryotic FGE.
  • High yields achieved (> 50 mg FGE/liter culture medium).
  • Single step purification.
  • Purified FGE shows good stability.
  • Production in selected eukaryotic cells.


  • Application for the production of individual sulfatases, the latter being used e.g. in enzyme substitution therapies in diseases like LSD.
  • Use to generate an aldehyde tag on a therapeutically active polypeptide of interest (e.g. an antibody for ADC).
  • Use as an inhibitor of furin or furin-like proteases.
  • Use as a diagnostic or therapeutic compound.
  • Therapy of Multiple Sulfatase Deficiency (MSD) through protein substitution therapy.

Developmental Status

Experimental, lead candidate identified.

Patent Status

A international patent application strategy is being prosecuted.


J Biol Chem 2013, 288(8), 5828-39.

Reference: BioT-1646-UMG

About MBM

MBM ScienceBridge GmbH is the technology transfer organization of the Georg-August University Goettingen. It is a spin-off of the Competence Center MBM, a technology transfer initiative within Georg-August-University formed in 2001, which was spun off into the MBM ScienceBridge GmbH in 2004. Their focus includes innovations from the areas of Medical and Measurement Technology, Biotechnology, Chemistry, Physics, Information Technology, Forestry and Agriculture.

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