Oxidoreductases;
Acting on a sulfur group of donors;
With oxygen as acceptor

[sulfatase]-L-cysteine:oxygen oxidoreductase (3-oxo-L-alanine-forming)

a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O [RN:R11878]

R11878

[sulfatase]-L-cysteine [CPD:C21740];
O2 [CPD:C00007];
a thiol

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.

EC 1.8.3.7 created 2014

1  [PMID:9342345]

Dierks T, Schmidt B, von Figura K

Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum.

Proc Natl Acad Sci U S A 94:11963-8 (1997)
DOI:10.1073/pnas.94.22.11963

2  [PMID:9748219]

Dierks T, Miech C, Hummerjohann J, Schmidt B, Kertesz MA, von Figura K

Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine.

J Biol Chem 273:25560-4 (1998)
DOI:10.1074/jbc.273.40.25560

3  [PMID:15657036]

Preusser-Kunze A, Mariappan M, Schmidt B, Gande SL, Mutenda K, Wenzel D, von Figura K, Dierks T

Molecular characterization of the human Calpha-formylglycine-generating enzyme.

J Biol Chem 280:14900-10 (2005)
DOI:10.1074/jbc.M413383200

[hsa:285362]

4  [PMID:16368756]

Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG

A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.

Proc Natl Acad Sci U S A 103:81-6 (2006)
DOI:10.1073/pnas.0507592102

[hsa:285362]

5  [PMID:18390551]

Carlson BL, Ballister ER, Skordalakes E, King DS, Breidenbach MA, Gilmore SA, Berger JM, Bertozzi CR

Function and structure of a prokaryotic formylglycine-generating enzyme.

J Biol Chem 283:20117-25 (2008)
DOI:10.1074/jbc.M800217200

[mtu:Rv0712] [sco:SCO7548]

6  [PMID:25931126]

Holder PG, Jones LC, Drake PM, Barfield RM, Banas S, de Hart GW, Baker J, Rabuka D

Reconstitution of Formylglycine-generating Enzyme with Copper(II) for Aldehyde Tag Conversion.

J Biol Chem 290:15730-45 (2015)
DOI:10.1074/jbc.M115.652669

7  [PMID:26403223]

Knop M, Engi P, Lemnaru R, Seebeck FP

In Vitro Reconstitution of Formylglycine-Generating Enzymes Requires Copper(I).

Chembiochem 16:2147-50 (2015)
DOI:10.1002/cbic.201500322

8  [PMID:27862795]

Knop M, Dang TQ, Jeschke G, Seebeck FP

Copper is a Cofactor of the Formylglycine-Generating Enzyme.

Chembiochem 18:161-165 (2017)
DOI:10.1002/cbic.201600359

9  [PMID:28544744]

Meury M, Knop M, Seebeck FP

Structural Basis for Copper-Oxygen Mediated C-H Bond Activation by the Formylglycine-Generating Enzyme.

Angew Chem Int Ed Engl 56:8115-8119 (2017)
DOI:10.1002/anie.201702901

[tcu:Tcur_4811]