Search results for SUMF1

Showing 5 results out of 5

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Species

Types

Compartments

Reaction types

Search properties

Protein (1 results from a total of 1)

Identifier: R-HSA-1614316
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: SUMF1: Q8NBK3

Complex (1 results from a total of 1)

Identifier: R-HSA-1614330
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen

Reaction (2 results from a total of 2)

Identifier: R-HSA-1614362
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
The sulfatase-modifying factor 1 (SUMF1, also called C-alpha-formylglycine-generating enzyme, FGE) (Preusser-Kunze et al. 2005, Cosma et al. 2003, Landgrebe et al. 2003) oxidises the critical cysteine residue in arylsulfatases to an active site 3-oxoalanine residue thus confering sulfatase activity (Roeser et al. 2006). Defects in SUMF1 cause multiple sulfatase deficiency (MSD) (MIM:272200), an impairment of arylsulfatase activity due to defective post-translational modification of the cysteine residue (Cosma et al. 2003, Dierks et al, 2003). This post-translational modification is thought to be highly conserved in eukaryotes (Selmer et al. 1996, von Figura et al. 1998). SUMF1 is active as either a monomer or a homodimer. A monomer is described in this reaction.
Identifier: R-HSA-1614336
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Sulfatase-modifying factor 2 (SUMF2, also called C-alpha-formylglycine-generating enzyme 2, pFGE) is the paralogue of SUMF1. While SUMF1 can modify a critical residue on arylsulfatases to confer activity to them, SUMF2 lacks this ability (Mariappan et al. 2005) and instead, SUMF2 can inhibit the action of SUMF1 by dimerising with it (Zito et al. 2005). SUMF2 can interact with sulfatases with and without SUMF1 (Zito et al. 2005).

Pathway (1 results from a total of 1)

Identifier: R-HSA-1663150
Species: Homo sapiens
Sulfatase activity requires a unique posttranslational modification (PTM) of a catalytic cysteine residue into a formylglycine. This modification is impaired in patients with multiple sulfatase deficiency (MSD) due to defects in the SUMF1 (sulfatase-modifying factor 1) gene responsible for this PTM. SUMF2 can inhibit the activity of SUMF1 thereby providing a mechanism for the regulation of sulfatase activation (Ghosh 2007, Diez-Roux & Ballabio 2005).
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