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Enzyme Nomenclature
Information on EC 1.8.3.B2 - formylglycine generating enzyme
for references in articles please use BRENDA:EC1.8.3.B2
Word Map on EC 1.8.3.B2
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.8.3.B2
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
formylglycine generating enzyme
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
a [sulfatase]-L-cysteine:oxygen, acceptor oxidoreductase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
Ac-LCSPSRGSLFTGR-NH2 + O2 + reduced dithiothreitol
Ac-L-3-oxo-L-Ala-SPSRGSLFTGR-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
AC-MTDFYVPVSLCTPSRAALLTGRS-amide + O2 + reduced dithiothreitol
AC-MTDFYVPVSL-3-oxo-Ala-TPSRAALLTGRS-amide + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
[arylsulfatase A]-L-cysteine69 + O2 + reduced acceptor
[arylsulfatase A]-Calpha-formylglycine69 + hydrogen sulfide + acceptor
-
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
-
?
Ac-LCSPSRGSLFTGR-NH2 + O2 + reduced dithiothreitol
Ac-L-3-oxo-L-Ala-SPSRGSLFTGR-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
Ac-LCSPSRGSLFTGR-NH2 + O2 + reduced dithiothreitol
Ac-L-3-oxo-L-Ala-SPSRGSLFTGR-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu+
Cu2+
additional information
Cu+
copper-metalloenzyme, one equivalent of Cu+ per acive site. No other transition metals can replace copper
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
Abz-SALCSPTRA-NH2
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.52
Abz-SALCSPTRA-NH2
mutant enzyme S266A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.58
Abz-SALCSPTRA-NH2
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
Abz-SALCSPTRA-NH2
mutant enzyme S266A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.01
Abz-SALCSPTRA-NH2
-
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, pH 8.0
0.027
Abz-SALCSPTRA-NH2
-
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0
0.027
Abz-SALCSPTRA-NH2
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.07
Abz-SALCSPTRA-NH2
-
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0
0.07
Abz-SALCSPTRA-NH2
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0101
Abz-SALCSPTRA-NH2
mutant enzyme S290K, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
0.333
Abz-SALCSPTRA-NH2
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
1.7
Abz-SALCSPTRA-NH2
-
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, pH 8.0
8.17
Abz-SALCSPTRA-NH2
mutant enzyme S266A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
17
Abz-SALCSPTRA-NH2
-
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, pH 8.0
48.3
Abz-SALCSPTRA-NH2
-
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0
48.33
Abz-SALCSPTRA-NH2
wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0
333.3
Abz-SALCSPTRA-NH2
-
mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C187A/C231A/C284S/C298A
C187A/C231A/C284S/C298A
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ten-fold increased activity compared to wild-type
-
C187A/C231A/C284S/C298A
-
ten-fold increased activity compared to wild-type
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.3.B2)
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