Copper is a Cofactor of the Formylglycine‐Generating Enzyme
نویسندگان
چکیده
Formylglycine-generating enzyme (FGE) is an O2 -utilizing oxidase that converts specific cysteine residues of client proteins to formylglycine. We show that CuI is an integral cofactor of this enzyme and binds with high affinity (KD =of 10-17 m) to a pair of active-site cysteines. These findings establish FGE as a novel type of copper enzyme.
منابع مشابه
Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme.
In eukaryotes, sulfate esters are degraded by sulfatases, which possess a unique Calpha-formylglycine residue in their active site. The defect in post-translational formation of the Calpha-formylglycine residue causes a severe lysosomal storage disorder in humans. Recently, FGE (formylglycine-generating enzyme) has been identified as the protein required for this specific modification. Using se...
متن کاملA general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.
The formylglycine (FGly)-generating enzyme (FGE) uses molecular oxygen to oxidize a conserved cysteine residue in all eukaryotic sulfatases to the catalytically active FGly. Sulfatases degrade and remodel sulfate esters, and inactivity of FGE results in multiple sulfatase deficiency, a fatal disease. The previously determined FGE crystal structure revealed two crucial cysteine residues in the a...
متن کاملCharacterization of pFGE , the Paralog of the C - Formylglycine - generating Enzyme
pFGE is the paralog of the formylglycine-generating enzyme (FGE), which catalyzes the oxidation of a specific cysteine to C -formylglycine, the catalytic residue in the active site of sulfatases. The enzymatic activity of sulfatases depends on this posttranslational modification, and the genetic defect of FGE causes multiple sulfatase deficiency. The structural and functional properties of pFGE...
متن کاملEstablishment of molybdeum cofactor detection system in Escherichia coli
In the current study, in order to verify the presence of bacterial Molybdenum cofactor, an indirect approach was made by showing the activity of BisC enzyme as a reporter gene. The activity of the BisC enzyme is dependent to Bis-MGD cofactor. BisC enzyme converts biotin sulfoxide to biotin under abiotic stress condition and it can also reduce TMANO and because of this property it was applied on...
متن کاملNew Aldehyde Tag Sequences Identified by Screening Formylglycine Generating Enzymes in Vitro and in Vivo
Formylglycine generating enzyme (FGE) performs a critical posttranslational modification of type I sulfatases, converting cysteine within the motif CxPxR to the aldehyde-bearing residue formylglycine (FGly). This concise motif can be installed within heterologous proteins as a genetically encoded "aldehyde tag" for site-specific labeling with aminooxy- or hydrazide-functionalized probes. In thi...
متن کامل