Entry |
|
Name |
formylglycine-generating enzyme;
sulfatase-modifying factor 1;
Calpha-formylglycine-generating enzyme 1;
SUMF1 (gene name)
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Class |
Oxidoreductases;
Acting on a sulfur group of donors;
With oxygen as acceptor
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Sysname |
[sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming)
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Reaction(IUBMB) |
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O [RN: R11878]
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Reaction(KEGG) |
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Substrate |
[sulfatase]-L-cysteine [CPD: C21740];
O2 [CPD: C00007];
a thiol
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Product |
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Comment |
Requires a copper cofactor and Ca2+. The enzyme, which is found in both prokaryotes and eukaryotes, catalyses a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity. The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro. Glutathione alo acts in vitro, but it is not known whether it is used in vivo.
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History |
EC 1.8.3.7 created 2014
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Orthology |
K13444 | formylglycine-generating enzyme |
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Genes |
» show all
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Reference |
|
Authors |
Dierks T, Schmidt B, von Figura K |
Title |
Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. |
Journal |
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Reference |
|
Authors |
Dierks T, Miech C, Hummerjohann J, Schmidt B, Kertesz MA, von Figura K |
Title |
Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. |
Journal |
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Reference |
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Authors |
Preusser-Kunze A, Mariappan M, Schmidt B, Gande SL, Mutenda K, Wenzel D, von Figura K, Dierks T |
Title |
Molecular characterization of the human Calpha-formylglycine-generating enzyme. |
Journal |
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Sequence |
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Reference |
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Authors |
Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG |
Title |
A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. |
Journal |
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Sequence |
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Reference |
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Authors |
Carlson BL, Ballister ER, Skordalakes E, King DS, Breidenbach MA, Gilmore SA, Berger JM, Bertozzi CR |
Title |
Function and structure of a prokaryotic formylglycine-generating enzyme. |
Journal |
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Sequence |
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Reference |
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Authors |
Holder PG, Jones LC, Drake PM, Barfield RM, Banas S, de Hart GW, Baker J, Rabuka D |
Title |
Reconstitution of Formylglycine-generating Enzyme with Copper(II) for Aldehyde Tag Conversion. |
Journal |
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Reference |
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Authors |
Knop M, Engi P, Lemnaru R, Seebeck FP |
Title |
In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I). |
Journal |
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Reference |
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Authors |
Knop M, Dang TQ, Jeschke G, Seebeck FP |
Title |
Copper is a Cofactor of the Formylglycine-Generating Enzyme. |
Journal |
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Reference |
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Authors |
Meury M, Knop M, Seebeck FP |
Title |
Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme. |
Journal |
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Sequence |
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Other DBs |
ExplorEnz - The Enzyme Database: | 1.8.3.7 |
ExPASy - ENZYME nomenclature database: | 1.8.3.7 |
BRENDA, the Enzyme Database: | 1.8.3.7 |
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