1.8.3.7: formylglycine-generating enzyme
This is an abbreviated version!
For detailed information about formylglycine-generating enzyme, go to the full flat file.
Word Map on EC 1.8.3.7
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1.8.3.7
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sulfatases
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metachromatic
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mucopolysaccharidosis
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leukodystrophy
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ichthyosis
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antibody-drug
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ultra-rare
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morquio
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medicine
- 1.8.3.7
-
sulfatases
-
metachromatic
- mucopolysaccharidosis
- leukodystrophy
-
ichthyosis
-
antibody-drug
-
ultra-rare
- morquio
- medicine
Reaction
Synonyms
AtsB, C-alpha-formylglycine-generating enzyme 1, Calpha-formylglycine-generating enzyme, Calpha-formylglycine-generating enzyme 1, FGE, FGly-generating enzyme, formylglycine generating enzyme, sulfatase-modifying factor 1, SUMF1
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Metals Ions
Metals Ions on EC 1.8.3.7 - formylglycine-generating enzyme
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Ca2+
Cu(I)
Cu+
Cu2+
additional information
the enzyme binds the substrate directly at a mononuclear Cu(I) center to initiate O2 activation. The copper atom is coordinated by two active-site cysteine residues in a nearly linear geometry
Cu(I)
the enzyme (FGE) mediates O2-activation and hydrogen-atom abstraction in an active site that contains Cu(I) coordinated to two cysteine residues. The 1.04 A crystal structure of the enzyme in complex with copper and a cysteine-containing peptide substrate unveils a network of four crystallographic waters and two active site residues that form a highly acidic O2-binding pocket juxtaposed to the trigonal planar tris-cysteine coordinated Cu(I) center
Cu+
copper-metalloenzyme, one equivalent of Cu+ per acive site. No other transition metals can replace copper
the enzyme contains a copper cofactor. The purified enzyme requires preactivation with copper
Cu2+
the enzyme contains a copper cofactor. The purified enzyme requires preactivation with copper
additional information
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the enzyme does not require a divalent cation